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Conserved domains on  [gi|301609641|ref|XP_002934369|]
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nuclear factor of activated T-cells, cytoplasmic 4 [Xenopus tropicalis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHD-n super family cl08275
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 405-578 9.15e-119

N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel).


The actual alignment was detected with superfamily member cd07881:

Pssm-ID: 447596  Cd Length: 175  Bit Score: 362.59  E-value: 9.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  405 DWPLPSQFEGLELRVEMQPRTHHRAHYETEGSRGAVKASPGGHPVVKLSGYNE-KPITLQMFIGTADERNLRPHAFYQVH 483
Cdd:cd07881     1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  484 RITGKMVATPSYEALVGSTKVLEMSLLPENNMCANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGAGKG 563
Cdd:cd07881    81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                         170
                  ....*....|....*
gi 301609641  564 ISLQVASIPIECSQR 578
Cdd:cd07881   161 LSLQVASNPIECSQR 175
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 583-683 1.99e-45

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: 158.42  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  583 LPQVENYSLSACSVNGREELLICGSNFLSDSKVIFLEKGPDGKLQWEEEAKVNKLKSNESLLSVQVPEYCNKEITRPLQV 662
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 301609641  663 YFYISNGRRKRSPMQSFRYLP 683
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 771-969 1.57e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  771 PPVPTdfkcPPSYPENGSEVSLSLPFHSNSNPALPPSPVPWSPQPcsshSACASTFGGPLLPHLTQPSKLnetlavshen 850
Cdd:PHA03247 2766 PPAPA----PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD----PPAAVLAPAAALPPAASPAGP---------- 2827

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  851 ySASPNLAALEFDATAHPFSPAYQPFTTCAPPSyttlGDGERLGPTQP----VESSTLPIVSRVDQCTPVQQFPSNALPD 926
Cdd:PHA03247 2828 -LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG----GDVRRRPPSRSpaakPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 301609641  927 HQTNHLnsqvqkgravsqtvfATPSPSLPPSEEETAPQAFAPT 969
Cdd:PHA03247 2903 DQPERP---------------PQPQAPPPPQPQPQPPPPPQPQ 2930
 
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 ...
 405-578 9.15e-119

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: 362.59  E-value: 9.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  405 DWPLPSQFEGLELRVEMQPRTHHRAHYETEGSRGAVKASPGGHPVVKLSGYNE-KPITLQMFIGTADERNLRPHAFYQVH 483
Cdd:cd07881     1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  484 RITGKMVATPSYEALVGSTKVLEMSLLPENNMCANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGAGKG 563
Cdd:cd07881    81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                         170
                  ....*....|....*
gi 301609641  564 ISLQVASIPIECSQR 578
Cdd:cd07881   161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 583-683 1.99e-45

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: 158.42  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  583 LPQVENYSLSACSVNGREELLICGSNFLSDSKVIFLEKGPDGKLQWEEEAKVNKLKSNESLLSVQVPEYCNKEITRPLQV 662
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 301609641  663 YFYISNGRRKRSPMQSFRYLP 683
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 585-683 3.77e-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: 109.19  E-value: 3.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641   585 QVENYSLSACSVNGREELLICGSNFLS-DSKVIFLEKGpDGKLQWEEEAKVNKLKSNES-LLSVQVPEYCNKEITRPLQV 662
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTV 79

                           90       100
                   ....*....|....*....|..
gi 301609641   663 YFYISNGRRK-RSPMQSFRYLP 683
Cdd:pfam16179   80 NIQLRRPSDKaTSEPQPFTYLP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 417-576 2.22e-27

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: 109.32  E-value: 2.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641   417 LRVEMQPRTH-HRAHYETEG-SRGAVKA-----SPGGHPVVKLSGYNEKPItLQMFIGTADERnLRPHAfyqvHRITGKM 489
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDGPAV-IRVSLVTKDEP-HRPHP----HSLVGKD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641   490 VatpsyealvgSTKVLEMSLLPENnMCANIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLVF 552
Cdd:pfam00554   75 C----------KDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCF 143

                          170       180
                   ....*....|....*....|....*.
gi 301609641   553 RVHVP--QGAGKGISLQVASIPIECS 576
Cdd:pfam00554  144 QAFLPdtRGNFTTPLPPVVSNPIYDK 169
IPT smart00429
ig-like, plexins, transcription factors;
583-682 2.30e-09

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 55.12  E-value: 2.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641    583 LPQVENYSLSACSVNGREELLICGSNFLSDSKVIFLEKGpdgklqWEEEAKVnkLKSNESLLSVQVPEYCNKEITRPLQV 662
Cdd:smart00429    1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV------GEAPCTF--SPSSSTAIVCKTPPYHNIPGSVPVRT 72

                            90       100
                    ....*....|....*....|
gi 301609641    663 yFYISNGRRKRSPmQSFRYL 682
Cdd:smart00429   73 -VGLRNGGVPSSP-QPFTYV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-969 1.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  771 PPVPTdfkcPPSYPENGSEVSLSLPFHSNSNPALPPSPVPWSPQPcsshSACASTFGGPLLPHLTQPSKLnetlavshen 850
Cdd:PHA03247 2766 PPAPA----PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD----PPAAVLAPAAALPPAASPAGP---------- 2827

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  851 ySASPNLAALEFDATAHPFSPAYQPFTTCAPPSyttlGDGERLGPTQP----VESSTLPIVSRVDQCTPVQQFPSNALPD 926
Cdd:PHA03247 2828 -LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG----GDVRRRPPSRSpaakPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 301609641  927 HQTNHLnsqvqkgravsqtvfATPSPSLPPSEEETAPQAFAPT 969
Cdd:PHA03247 2903 DQPERP---------------PQPQAPPPPQPQPQPPPPPQPQ 2930
 
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 ...
 405-578 9.15e-119

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: 362.59  E-value: 9.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  405 DWPLPSQFEGLELRVEMQPRTHHRAHYETEGSRGAVKASPGGHPVVKLSGYNE-KPITLQMFIGTADERNLRPHAFYQVH 483
Cdd:cd07881     1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  484 RITGKMVATPSYEALVGSTKVLEMSLLPENNMCANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGAGKG 563
Cdd:cd07881    81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                         170
                  ....*....|....*
gi 301609641  564 ISLQVASIPIECSQR 578
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 ...
 416-577 7.89e-66

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: 219.07  E-value: 7.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  416 ELRVEMQPRTHHRAHYETEGSRGAVKASP-GGHPVVKLSGYNEkPITLQMFIGTADERnLRPHAFYQVHRITGKmVATPS 494
Cdd:cd07927     2 ELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGYME-PVGLQVFIGTASGR-LKPHAFYQVHRITGK-TTTPC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  495 YEALVGSTKVLEMSLLPENNMCANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGAGKGISLQVASIPIE 574
Cdd:cd07927    79 KEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIE 158


                  ...
gi 301609641  575 CSQ 577
Cdd:cd07927   159 CSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 416-577 6.87e-53

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: 182.33  E-value: 6.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  416 ELRVEMQPRTHHRAHYETEGSRGAVKASPG-GHPVVKLSGYNeKPITLQMFIGTaDERNLRPHAFYQVHRITGKMvATPS 494
Cdd:cd07882     2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGYN-KPVVLQVFVGT-DSGRVKPHGFYQACKVTGRN-TTPC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  495 YEALVGSTKVLEMSLLPENNMCANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGAGKGISLQVASIPIE 574
Cdd:cd07882    79 EEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPIL 158


                  ...
gi 301609641  575 CSQ 577
Cdd:cd07882   159 CTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 583-683 1.99e-45

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: 158.42  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  583 LPQVENYSLSACSVNGREELLICGSNFLSDSKVIFLEKGPDGKLQWEEEAKVNKLKSNESLLSVQVPEYCNKEITRPLQV 662
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 301609641  663 YFYISNGRRKRSPMQSFRYLP 683
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 416-577 3.79e-31

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: 120.55  E-value: 3.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  416 ELRVEMQPRTH-HRAHYETEG-SRGAVK-----ASPGGHPVVKLSGYNEkPITLQMFIGTADERnLRPHAfYQVHRITGK 488
Cdd:cd07827     2 YLEITEQPKQRgHRFRYECEGrSAGSIPgenstADRKTFPTVKLRNYNG-PAKIVVSLVTKDDP-PKPHP-HQLVGKTDC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  489 mvatpsyealvgSTKVLEMSLLPENNMCANIDCAGILKLRNSDIELRKGETD-----------------IGRKNTRVRLV 551
Cdd:cd07827    79 ------------RDGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLC 146

                         170       180
                  ....*....|....*....|....*...
gi 301609641  552 FRVHVPQGAGKGISL--QVASIPIECSQ 577
Cdd:cd07827   147 FQAFIEDSDGGFTLPlpPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 585-683 3.77e-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: 109.19  E-value: 3.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641   585 QVENYSLSACSVNGREELLICGSNFLS-DSKVIFLEKGpDGKLQWEEEAKVNKLKSNES-LLSVQVPEYCNKEITRPLQV 662
Cdd:pfam16179    1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQvAIVFKTPPYRDPDITEPVTV 79

                           90       100
                   ....*....|....*....|..
gi 301609641   663 YFYISNGRRK-RSPMQSFRYLP 683
Cdd:pfam16179   80 NIQLRRPSDKaTSEPQPFTYLP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 417-576 2.22e-27

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: 109.32  E-value: 2.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641   417 LRVEMQPRTH-HRAHYETEG-SRGAVKA-----SPGGHPVVKLSGYNEKPItLQMFIGTADERnLRPHAfyqvHRITGKM 489
Cdd:pfam00554    1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDGPAV-IRVSLVTKDEP-HRPHP----HSLVGKD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641   490 VatpsyealvgSTKVLEMSLLPENnMCANIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLVF 552
Cdd:pfam00554   75 C----------KDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCF 143

                          170       180
                   ....*....|....*....|....*.
gi 301609641   553 RVHVP--QGAGKGISLQVASIPIECS 576
Cdd:pfam00554  144 QAFLPdtRGNFTTPLPPVVSNPIYDK 169
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 584-683 4.25e-24

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: 97.74  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  584 PQVENYSLSACSVNGREELLICGSNFLS-DSKVIFLEKGPdGKLQWEEEAKVNKLKSNESLLSVQVPEYCNKEITRPLQV 662
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKpDIKVWFGEKGP-GETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79

                          90       100
                  ....*....|....*....|..
gi 301609641  663 YFYISNGR-RKRSPMQSFRYLP 683
Cdd:cd00602    80 PIQLVRPDdRKRSEPLTFTYTP 101
IPT smart00429
ig-like, plexins, transcription factors;
583-682 2.30e-09

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 55.12  E-value: 2.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641    583 LPQVENYSLSACSVNGREELLICGSNFLSDSKVIFLEKGpdgklqWEEEAKVnkLKSNESLLSVQVPEYCNKEITRPLQV 662
Cdd:smart00429    1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV------GEAPCTF--SPSSSTAIVCKTPPYHNIPGSVPVRT 72

                            90       100
                    ....*....|....*....|
gi 301609641    663 yFYISNGRRKRSPmQSFRYL 682
Cdd:smart00429   73 -VGLRNGGVPSSP-QPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 584-683 8.58e-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: 45.14  E-value: 8.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  584 PQVENYSLSACSVNGREELLICGSNFLS--DSKVIFLEKGPdgklqweeeakVNKLKSNESLLSVQVPEYCNKeitRPLQ 661
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSgsNLRVTFGGGVP-----------CSVLSVSSTAIVCTTPPYANP---GPGP 66

                          90       100
                  ....*....|....*....|...
gi 301609641  662 VYFYISNGR-RKRSPMQSFRYLP 683
Cdd:cd00102    67 VEVTVDRGNgGITSSPLTFTYVP 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-969 1.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  771 PPVPTdfkcPPSYPENGSEVSLSLPFHSNSNPALPPSPVPWSPQPcsshSACASTFGGPLLPHLTQPSKLnetlavshen 850
Cdd:PHA03247 2766 PPAPA----PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD----PPAAVLAPAAALPPAASPAGP---------- 2827

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301609641  851 ySASPNLAALEFDATAHPFSPAYQPFTTCAPPSyttlGDGERLGPTQP----VESSTLPIVSRVDQCTPVQQFPSNALPD 926
Cdd:PHA03247 2828 -LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG----GDVRRRPPSRSpaakPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 301609641  927 HQTNHLnsqvqkgravsqtvfATPSPSLPPSEEETAPQAFAPT 969
Cdd:PHA03247 2903 DQPERP---------------PQPQAPPPPQPQPQPPPPPQPQ 2930
 
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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