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Conserved domains on  [gi|27886520|ref|NP_619728|]
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nuclear factor of activated T-cells 5 isoform a [Homo sapiens]

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 ...
 204-364 3.24e-107

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


:

Pssm-ID: 143642  Cd Length: 161  Bit Score: 336.41  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  204 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 283
Cdd:cd07882    1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  284 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNIMRKDGSTLTLQTPSSPILCT 363
Cdd:cd07882   81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                 .
gi 27886520  364 Q 364
Cdd:cd07882  161 Q 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 368-467 1.20e-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: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  368 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 446
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                         90       100
                 ....*....|....*....|.
gi 27886520  447 GIYVVTNAGRSHDVQPFTYTP 467
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1111-1247 8.79e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.87  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520   1111 PISHIQTPMLSQEQAQPPQQGLFQPQVALGSLPPNPMPQSQQGTMFQSQHSIVAMQSNSPSQEQQQQQQQQQQQQQQQQQ 1190
Cdd:pfam09770  221 PPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPT 300

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27886520   1191 SILfsnQNTMATMASPKQPPPNMIFNPNQNPMANQEQQNQSIFHQ------QSNMAPMNQEQQ 1247
Cdd:pfam09770  301 QIL---QNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQapiithPQQLAQLSEEEK 360
 
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 ...
 204-364 3.24e-107

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


Pssm-ID: 143642  Cd Length: 161  Bit Score: 336.41  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  204 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 283
Cdd:cd07882    1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  284 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNIMRKDGSTLTLQTPSSPILCT 363
Cdd:cd07882   81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                 .
gi 27886520  364 Q 364
Cdd:cd07882  161 Q 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 368-467 1.20e-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: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  368 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 446
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                         90       100
                 ....*....|....*....|.
gi 27886520  447 GIYVVTNAGRSHDVQPFTYTP 467
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 370-468 3.79e-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: 3.79e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520    370 EILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQN-HLIVKVPPYHDQHITLPVSVG 447
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTVN 80

                           90       100
                   ....*....|....*....|..
gi 27886520    448 IYVVTNAGR-SHDVQPFTYTPD 468
Cdd:pfam16179   81 IQLRRPSDKaTSEPQPFTYLPL 102
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 206-363 4.25e-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: 100.46  E-value: 4.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520    206 LKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHgfyqACRVTGRNtt 279
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPH----PHSLVGKD-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520    280 pCKevdiEGTTVIEVGldpSNNMTLAVDCVGILKLRNADVEARIG------------IAGSKKKS-----TRARLVFRVN 342
Cdd:pfam00554   75 -CK----DGVCEVELG---PEDMVASFQNLGIQCVKKKDVEEALKerielnidpfnvGFEALRQIkdmdlNVVRLCFQAF 146

                          170       180
                   ....*....|....*....|...
gi 27886520    343 IMRKDGSTLTLQTP--SSPILCT 363
Cdd:pfam00554  147 LPDTRGNFTTPLPPvvSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
369-466 1.51e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 1.51e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520     369 PEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVsdensWKSEAEIDMElfHQNHLIVKVPPYHDQHITLPVS-VG 447
Cdd:smart00429    2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV-----GEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRtVG 74

                            90
                    ....*....|....*....
gi 27886520     448 IYvvtNAGRSHDVQPFTYT 466
Cdd:smart00429   75 LR---NGGVPSSPQPFTYV 90
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1111-1247 8.79e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.87  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520   1111 PISHIQTPMLSQEQAQPPQQGLFQPQVALGSLPPNPMPQSQQGTMFQSQHSIVAMQSNSPSQEQQQQQQQQQQQQQQQQQ 1190
Cdd:pfam09770  221 PPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPT 300

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27886520   1191 SILfsnQNTMATMASPKQPPPNMIFNPNQNPMANQEQQNQSIFHQ------QSNMAPMNQEQQ 1247
Cdd:pfam09770  301 QIL---QNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQapiithPQQLAQLSEEEK 360
 
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 ...
 204-364 3.24e-107

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


Pssm-ID: 143642  Cd Length: 161  Bit Score: 336.41  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  204 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 283
Cdd:cd07882    1 KELKILVQPETQHRARYLTEGSRGSVKDRSQQGFPTVKLEGYNKPVVLQVFVGTDSGRVKPHGFYQACKVTGRNTTPCEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  284 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNIMRKDGSTLTLQTPSSPILCT 363
Cdd:cd07882   81 VDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPILCT 160


                 .
gi 27886520  364 Q 364
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 ...
 204-364 3.75e-91

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: 291.87  E-value: 3.75e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  204 KELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKE 283
Cdd:cd07927    1 YELRIEVQPEPHHRARYETEGSRGAVKAPSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRITGKTTTPCKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  284 VDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNIMRKDGSTLTLQTPSSPILCT 363
Cdd:cd07927   81 KIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIECS 160


                 .
gi 27886520  364 Q 364
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 ...
 196-364 5.27e-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: 183.47  E-value: 5.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  196 QYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQqGFPTVKLEGHNE--PVVLQVFVGNDSGR-VKPHGFYQACR 272
Cdd:cd07881    3 PLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTG-GHPVVQLHGYMEnkPLTLQMFIGTADDRyLRPHAFYQVHR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  273 VTGRN-TTPCKEVDIEGTTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNIMRKDGSTL 351
Cdd:cd07881   82 ITGKTvATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRVL 161

                        170
                 ....*....|...
gi 27886520  352 TLQTPSSPILCTQ 364
Cdd:cd07881  162 SLQVASNPIECSQ 174
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 368-467 1.20e-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: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  368 VPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSD-ENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSV 446
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDgEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                         90       100
                 ....*....|....*....|.
gi 27886520  447 GIYVVTNAGRSHDVQPFTYTP 467
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 204-364 5.68e-46

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: 163.31  E-value: 5.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  204 KELKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGfYQACRVTGrn 277
Cdd:cd07827    1 PYLEITEQPKQRgHRFRYECEGrSAGSIPGenstADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHP-HQLVGKTD-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  278 ttpCKEvdiegtTVIEVGLDPSNNMTLAVDCVGILKLRNADVEARIGIAG-----------------SKKKSTRARLVFR 340
Cdd:cd07827   78 ---CRD------GVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLCFQ 148

                        170       180
                 ....*....|....*....|....*.
gi 27886520  341 VNIMRKDG-STLTL-QTPSSPILCTQ 364
Cdd:cd07827  149 AFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 370-468 3.79e-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: 3.79e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520    370 EILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQN-HLIVKVPPYHDQHITLPVSVG 447
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTVN 80

                           90       100
                   ....*....|....*....|..
gi 27886520    448 IYVVTNAGR-SHDVQPFTYTPD 468
Cdd:pfam16179   81 IQLRRPSDKaTSEPQPFTYLPL 102
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 369-467 2.11e-37

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 135.87  E-value: 2.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  369 PEILKKSLHSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVG 447
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKpDIKVWFGEKGPGETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQVP 80

                         90       100
                 ....*....|....*....|..
gi 27886520  448 IYVVTNAG--RShDVQPFTYTP 467
Cdd:cd00602   81 IQLVRPDDrkRS-EPLTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 206-363 4.25e-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: 100.46  E-value: 4.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520    206 LKIVVQPETQ-HRARYLTEG-SRGSVKD----RTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHgfyqACRVTGRNtt 279
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPH----PHSLVGKD-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520    280 pCKevdiEGTTVIEVGldpSNNMTLAVDCVGILKLRNADVEARIG------------IAGSKKKS-----TRARLVFRVN 342
Cdd:pfam00554   75 -CK----DGVCEVELG---PEDMVASFQNLGIQCVKKKDVEEALKerielnidpfnvGFEALRQIkdmdlNVVRLCFQAF 146

                          170       180
                   ....*....|....*....|...
gi 27886520    343 IMRKDGSTLTLQTP--SSPILCT 363
Cdd:pfam00554  147 LPDTRGNFTTPLPPvvSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
369-466 1.51e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 1.51e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520     369 PEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVsdensWKSEAEIDMElfHQNHLIVKVPPYHDQHITLPVS-VG 447
Cdd:smart00429    2 PVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV-----GEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRtVG 74

                            90
                    ....*....|....*....
gi 27886520     448 IYvvtNAGRSHDVQPFTYT 466
Cdd:smart00429   75 LR---NGGVPSSPQPFTYV 90
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 377-467 4.20e-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: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  377 HSCSVKGEEEVFLIGKNFLK-GTKVIFQENVSDENSWKSEAEIDMELFHQNHLIV-KVPPYHDQHITLPVSVGIYVV-TN 453
Cdd:cd01177    9 TSGSVKGGDEVYLLCDKVQKeDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVfRTPPYHDPDITEPVKVKIQLKrPS 88

                         90
                 ....*....|....
gi 27886520  454 AGRSHDVQPFTYTP 467
Cdd:cd01177   89 DGERSESVPFTYVP 102
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 369-467 1.91e-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: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520  369 PEILKKSLHSCSVKGEEEVFLIGKNFLKG--TKVIFQENVsdenswkseaEIDMELFHQNHLIVKVPPYHDQHitlPVSV 446
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGsnLRVTFGGGV----------PCSVLSVSSTAIVCTTPPYANPG---PGPV 67

                         90       100
                 ....*....|....*....|..
gi 27886520  447 GIYVVT-NAGRSHDVQPFTYTP 467
Cdd:cd00102   68 EVTVDRgNGGITSSPLTFTYVP 89
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 206-265 1.64e-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: 46.65  E-value: 1.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27886520  206 LKIVVQPETQHRARYLTE--GSRGSVK----DRTQQGFPTVKLEGHNEPVV--LQVFVGNDSGRvKPH 265
Cdd:cd07884    3 LRIVEQPVDKFRFRYKSEmhGTHGSLLgersTSSKKTFPTVKLCNYRGQAVirCSLYQADDNRR-KPH 69
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1111-1247 8.79e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.87  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886520   1111 PISHIQTPMLSQEQAQPPQQGLFQPQVALGSLPPNPMPQSQQGTMFQSQHSIVAMQSNSPSQEQQQQQQQQQQQQQQQQQ 1190
Cdd:pfam09770  221 PPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPT 300

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27886520   1191 SILfsnQNTMATMASPKQPPPNMIFNPNQNPMANQEQQNQSIFHQ------QSNMAPMNQEQQ 1247
Cdd:pfam09770  301 QIL---QNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQapiithPQQLAQLSEEEK 360
 
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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