NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|195927856|gb|ACG55587|]
View 

nuclear factor of activated T-cells c1 isoform IA-IXL [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
417-591 1.32e-130

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: 389.94  E-value: 1.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 417 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVH 496
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 497 RITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRT 576
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                        170
                 ....*....|....*
gi 195927856 577 LSLQVASNPIECSQR 591
Cdd:cd07881  161 LSLQVASNPIECSQR 175
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
596-696 5.11e-44

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: 154.18  E-value: 5.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 596 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 675
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80
                         90       100
                 ....*....|....*....|.
gi 195927856 676 SFYVCNGKRKRSQYQRFTYLP 696
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
696-889 2.47e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  696 PANVPIIKTEPTDDFEPALTCGPMS--------QGISP-LPRPYYS------QQLTMPPDPGSCLVAGFAPCSQRNTLM- 759
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPApappaapaAGPPRrLTRPAVAslsesrESLPSPWDPADPPAAVLAPAAALPPAAs 2823
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  760 PTPPNASPKLHDLSSPAYTKGLTNPGHSGHLGLQP--PASEAPTmqevPRPMAIQPNSPEQPPSARL-QPQVSPHLNSsc 836
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPP----SRSPAAKPAAPARPPVRRLaRPAVSRSTES-- 2897
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195927856  837 plgrrQVLCPNSPSSPLPSAAQEPACLQSSALPPDMghRQPQPQKVQRNESPA 889
Cdd:PHA03247 2898 -----FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPL 2943
PHA03247 super family cl33720
large tegument protein UL36; Provisional
7-298 5.10e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856    7 PVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEEEHYSYVSPSvTSTLPLPTAHSALPAACHDLQTSTPGISAVPSAN 86
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856   87 HPPS--------YGGAVdsGPSGYFLSSGNTRPNGAPTLESPRIEITSylglhhgsgqffhdvevedvLPSCKRSPSTAT 158
Cdd:PHA03247 2840 PPPPgppppslpLGGSV--APGGDVRRRPPSRSPAAKPAAPARPPVRR--------------------LARPAVSRSTES 2897
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  159 LHLPSLEAYRDPSCLSPASSLSSRSCNSEASsyesnysyPYASPQTSPWQSPCVSPKTTDPEEGFPRSLGACHLLGSPRH 238
Cdd:PHA03247 2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--------PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  239 SPSTSPRASITEeswlgARGSRPTSPcnkrkyslngrqpscsphhSPTPSPHGSPRVSVT 298
Cdd:PHA03247 2970 GRVAVPRFRVPQ-----PAPSREAPA-------------------SSTPPLTGHSLSRVS 3005
 
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 ...
417-591 1.32e-130

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: 389.94  E-value: 1.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 417 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVH 496
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 497 RITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRT 576
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                        170
                 ....*....|....*
gi 195927856 577 LSLQVASNPIECSQR 591
Cdd:cd07881  161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
596-696 5.11e-44

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: 154.18  E-value: 5.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 596 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 675
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80
                         90       100
                 ....*....|....*....|.
gi 195927856 676 SFYVCNGKRKRSQYQRFTYLP 696
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
429-589 3.95e-37

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: 137.05  E-value: 3.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  429 LRIEVQPKSH-HRAHYETEG-SRGAVKA-----SAGGHPIVQLHGYLEnePLTLQLFIGTADDRLlRPHAfyqvHRITGK 501
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDG--PAVIRVSLVTKDEPH-RPHP----HSLVGK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  502 TvsttsheiilSNTKVLEIPLLPENnMRAIIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLV 564
Cdd:pfam00554  74 D----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142
                         170       180
                  ....*....|....*....|....*..
gi 195927856  565 FRVHIP--QPNGRTLSLQVASNPIECS 589
Cdd:pfam00554 143 FQAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
599-696 4.35e-28

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: 108.80  E-value: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  599 VEKQSTDSYPVIGGKKMVLSGHNFL-QDSKVIFVEKApDGHHVWEMEAKTDRDLCKPNS-LVVEIPPFRNQRITSPVQVS 676
Cdd:pfam16179   2 ICRLSLCSGSVTGGEEIILLCEKVLkDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|.
gi 195927856  677 FYVCNGKRK-RSQYQRFTYLP 696
Cdd:pfam16179  81 IQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
596-695 1.84e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 60.90  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856   596 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFvekapdGHHVWEMEAKTDRDlcKPNSLVVEIPPFRNQRITSPVQV 675
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFV------EVGVGEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRT 72
                           90       100
                   ....*....|....*....|
gi 195927856   676 sFYVCNGKRkRSQYQRFTYL 695
Cdd:smart00429  73 -VGLRNGGV-PSSPQPFTYV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
696-889 2.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  696 PANVPIIKTEPTDDFEPALTCGPMS--------QGISP-LPRPYYS------QQLTMPPDPGSCLVAGFAPCSQRNTLM- 759
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPApappaapaAGPPRrLTRPAVAslsesrESLPSPWDPADPPAAVLAPAAALPPAAs 2823
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  760 PTPPNASPKLHDLSSPAYTKGLTNPGHSGHLGLQP--PASEAPTmqevPRPMAIQPNSPEQPPSARL-QPQVSPHLNSsc 836
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPP----SRSPAAKPAAPARPPVRRLaRPAVSRSTES-- 2897
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195927856  837 plgrrQVLCPNSPSSPLPSAAQEPACLQSSALPPDMghRQPQPQKVQRNESPA 889
Cdd:PHA03247 2898 -----FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPL 2943
PHA03247 PHA03247
large tegument protein UL36; Provisional
7-298 5.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856    7 PVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEEEHYSYVSPSvTSTLPLPTAHSALPAACHDLQTSTPGISAVPSAN 86
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856   87 HPPS--------YGGAVdsGPSGYFLSSGNTRPNGAPTLESPRIEITSylglhhgsgqffhdvevedvLPSCKRSPSTAT 158
Cdd:PHA03247 2840 PPPPgppppslpLGGSV--APGGDVRRRPPSRSPAAKPAAPARPPVRR--------------------LARPAVSRSTES 2897
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  159 LHLPSLEAYRDPSCLSPASSLSSRSCNSEASsyesnysyPYASPQTSPWQSPCVSPKTTDPEEGFPRSLGACHLLGSPRH 238
Cdd:PHA03247 2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--------PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  239 SPSTSPRASITEeswlgARGSRPTSPcnkrkyslngrqpscsphhSPTPSPHGSPRVSVT 298
Cdd:PHA03247 2970 GRVAVPRFRVPQ-----PAPSREAPA-------------------SSTPPLTGHSLSRVS 3005
 
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 ...
417-591 1.32e-130

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: 389.94  E-value: 1.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 417 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVH 496
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 497 RITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRT 576
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                        170
                 ....*....|....*
gi 195927856 577 LSLQVASNPIECSQR 591
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 ...
427-590 2.11e-72

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: 235.63  E-value: 2.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 427 YELRIEVQPKSHHRAHYETEGSRGAVKASA-GGHPIVQLHGYleNEPLTLQLFIGTADDRLlRPHAFYQVHRITGKTvST 505
Cdd:cd07927    1 YELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGY--MEPVGLQVFIGTASGRL-KPHAFYQVHRITGKT-TT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 506 TSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRTLSLQVASNP 585
Cdd:cd07927   77 PCKEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNP 156

                 ....*
gi 195927856 586 IECSQ 590
Cdd:cd07927  157 IECSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
428-590 4.05e-58

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: 196.58  E-value: 4.05e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 428 ELRIEVQPKSHHRAHYETEGSRGAVKASAG-GHPIVQLHGYleNEPLTLQLFIGTADDRLlRPHAFYQVHRITGKTvSTT 506
Cdd:cd07882    2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGY--NKPVVLQVFVGTDSGRV-KPHGFYQACKVTGRN-TTP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 507 SHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRTLSLQVASNPI 586
Cdd:cd07882   78 CEEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157

                 ....
gi 195927856 587 ECSQ 590
Cdd:cd07882  158 LCTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
596-696 5.11e-44

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: 154.18  E-value: 5.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 596 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 675
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80
                         90       100
                 ....*....|....*....|.
gi 195927856 676 SFYVCNGKRKRSQYQRFTYLP 696
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
429-589 3.95e-37

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: 137.05  E-value: 3.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  429 LRIEVQPKSH-HRAHYETEG-SRGAVKA-----SAGGHPIVQLHGYLEnePLTLQLFIGTADDRLlRPHAfyqvHRITGK 501
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDG--PAVIRVSLVTKDEPH-RPHP----HSLVGK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  502 TvsttsheiilSNTKVLEIPLLPENnMRAIIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLV 564
Cdd:pfam00554  74 D----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142
                         170       180
                  ....*....|....*....|....*..
gi 195927856  565 FRVHIP--QPNGRTLSLQVASNPIECS 589
Cdd:pfam00554 143 FQAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
427-590 6.41e-37

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: 136.73  E-value: 6.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 427 YELRIEVQPKSH-HRAHYETEG-SRGAVK-----ASAGGHPIVQLHGYleNEPLTLQLFIGTADDRLlRPHAfYQVHRIT 499
Cdd:cd07827    1 PYLEITEQPKQRgHRFRYECEGrSAGSIPgenstADRKTFPTVKLRNY--NGPAKIVVSLVTKDDPP-KPHP-HQLVGKT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 500 GKTvsttsheiilsnTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETD-----------------IGRKNTRVR 562
Cdd:cd07827   77 DCR------------DGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVR 144
                        170       180       190
                 ....*....|....*....|....*....|
gi 195927856 563 LVFRVHIPQPNG-RTLSL-QVASNPIECSQ 590
Cdd:cd07827  145 LCFQAFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
599-696 4.35e-28

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: 108.80  E-value: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  599 VEKQSTDSYPVIGGKKMVLSGHNFL-QDSKVIFVEKApDGHHVWEMEAKTDRDLCKPNS-LVVEIPPFRNQRITSPVQVS 676
Cdd:pfam16179   2 ICRLSLCSGSVTGGEEIILLCEKVLkDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|.
gi 195927856  677 FYVCNGKRK-RSQYQRFTYLP 696
Cdd:pfam16179  81 IQLRRPSDKaTSEPQPFTYLP 101
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
597-696 8.13e-26

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: 102.36  E-value: 8.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 597 PLVEKQSTDSYPVIGGKKMVLSGHNFL-QDSKVIFVEKAPdGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 675
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNkPDIKVWFGEKGP-GETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79
                         90       100
                 ....*....|....*....|..
gi 195927856 676 SFYVCNG-KRKRSQYQRFTYLP 696
Cdd:cd00602   80 PIQLVRPdDRKRSEPLTFTYTP 101
IPT smart00429
ig-like, plexins, transcription factors;
596-695 1.84e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 60.90  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856   596 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFvekapdGHHVWEMEAKTDRDlcKPNSLVVEIPPFRNQRITSPVQV 675
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFV------EVGVGEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRT 72
                           90       100
                   ....*....|....*....|
gi 195927856   676 sFYVCNGKRkRSQYQRFTYL 695
Cdd:smart00429  73 -VGLRNGGV-PSSPQPFTYV 90
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
426-586 3.84e-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: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 426 PYeLRIEVQPKSHHRAHYETE--GSRGAVKA-----SAGGHPIVQLHGYleNEPLTLQLFIGTADDRLLRPHafyqVHRI 498
Cdd:cd07884    1 PF-LRIVEQPVDKFRFRYKSEmhGTHGSLLGerstsSKKTFPTVKLCNY--RGQAVIRCSLYQADDNRRKPH----VHKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 499 TGKTVSTTSHEIILSNTKvleipllPENNMRAIIDCAGIL---KLRNSDIELRKGETDIgrknTRVRLVFRVHIPQPNG- 574
Cdd:cd07884   74 VGKQGDDDVCDPHDIEVS-------PEGDYVAMFQNMGIIhtaKKNIPEELYKKKNMNL----NQVVLRFQAFAVSANGh 142
                        170
                 ....*....|...
gi 195927856 575 -RTLSLQVASNPI 586
Cdd:cd07884  143 lRPICPPVYSNPI 155
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
597-696 5.07e-06

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: 45.53  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856 597 PLVEKQSTDSYPVIGGKKMVLSGHNFL--QDSKVIFVEKAPdghhvwemeakTDRDLCKPNSLVVEIPPFRNQritSPVQ 674
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGsgSNLRVTFGGGVP-----------CSVLSVSSTAIVCTTPPYANP---GPGP 66
                         90       100
                 ....*....|....*....|...
gi 195927856 675 VSFYVCN-GKRKRSQYQRFTYLP 696
Cdd:cd00102   67 VEVTVDRgNGGITSSPLTFTYVP 89
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
625-696 2.42e-03

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: 38.45  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195927856 625 DSKVIFVEKAPDGHhVWEMEAK-TDRDLCKPNSLVVEIPPFRNQRITSPVQVSFYVcngKRKRSQYQR----FTYLP 696
Cdd:cd01177   30 DIQVRFFEEDEEET-VWEAFGDfSQTDVHRQYAIVFRTPPYHDPDITEPVKVKIQL---KRPSDGERSesvpFTYVP 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
696-889 2.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  696 PANVPIIKTEPTDDFEPALTCGPMS--------QGISP-LPRPYYS------QQLTMPPDPGSCLVAGFAPCSQRNTLM- 759
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPApappaapaAGPPRrLTRPAVAslsesrESLPSPWDPADPPAAVLAPAAALPPAAs 2823
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  760 PTPPNASPKLHDLSSPAYTKGLTNPGHSGHLGLQP--PASEAPTmqevPRPMAIQPNSPEQPPSARL-QPQVSPHLNSsc 836
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPP----SRSPAAKPAAPARPPVRRLaRPAVSRSTES-- 2897
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195927856  837 plgrrQVLCPNSPSSPLPSAAQEPACLQSSALPPDMghRQPQPQKVQRNESPA 889
Cdd:PHA03247 2898 -----FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPL 2943
PHA03247 PHA03247
large tegument protein UL36; Provisional
7-298 5.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856    7 PVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEEEHYSYVSPSvTSTLPLPTAHSALPAACHDLQTSTPGISAVPSAN 86
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856   87 HPPS--------YGGAVdsGPSGYFLSSGNTRPNGAPTLESPRIEITSylglhhgsgqffhdvevedvLPSCKRSPSTAT 158
Cdd:PHA03247 2840 PPPPgppppslpLGGSV--APGGDVRRRPPSRSPAAKPAAPARPPVRR--------------------LARPAVSRSTES 2897
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  159 LHLPSLEAYRDPSCLSPASSLSSRSCNSEASsyesnysyPYASPQTSPWQSPCVSPKTTDPEEGFPRSLGACHLLGSPRH 238
Cdd:PHA03247 2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--------PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927856  239 SPSTSPRASITEeswlgARGSRPTSPcnkrkyslngrqpscsphhSPTPSPHGSPRVSVT 298
Cdd:PHA03247 2970 GRVAVPRFRVPQ-----PAPSREAPA-------------------SSTPPLTGHSLSRVS 3005
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH