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Conserved domains on  [gi|27886563|ref|NP_004545|]
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nuclear factor of activated T-cells, cytoplasmic 4 isoform 2 [Homo sapiens]

Protein Classification

RHD-n_NFAT and IPT_NFAT domain-containing protein( domain architecture ID 10167651)

protein containing domains PHA03247, RHD-n_NFAT, and IPT_NFAT

Graphical summary

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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 ...
 407-580 5.69e-125

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: 374.53  E-value: 5.69e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 407 DWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYSE-KPLTLQMFIGTADERNLRPHAFYQVH 485
Cdd:cd07881   1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 486 RITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKV 565
Cdd:cd07881  81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                       170
                ....*....|....*
gi 27886563 566 VSVQAASVPIECSQR 580
Cdd:cd07881 161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 585-685 2.41e-53

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: 180.37  E-value: 2.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 585 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 664
Cdd:cd01178   1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                        90       100
                ....*....|....*....|.
gi 27886563 665 YFYVSNGRRKRSPTQSFRFLP 685
Cdd:cd01178  81 QFYVVNGKRKRSQPQTFTYTP 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 214-413 6.51e-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: 43.77  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   214 PLPSPRASPRPWTPEDPWSLYGPSPGGRGPEdswlLLSAPGPTPASPRPASPCGKRRYSSSGTPS-SASPALSRRGSLGE 292
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   293 EGSEPPPPPPLPLARDPGSPGPFDYVGAPPAESIPQKTRRTSSEQA-------VALPRSEEPASCNGKLPLGAEESVAPP 365
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptSAQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 27886563   366 GGSRKEVAGMDYLAVPSPLAWSKARIGGHSPIFRTS---ALPPLDWPLPSQ 413
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQPERPPQ 2910
 
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 ...
 407-580 5.69e-125

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: 374.53  E-value: 5.69e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 407 DWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYSE-KPLTLQMFIGTADERNLRPHAFYQVH 485
Cdd:cd07881   1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 486 RITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKV 565
Cdd:cd07881  81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                       170
                ....*....|....*
gi 27886563 566 VSVQAASVPIECSQR 580
Cdd:cd07881 161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 585-685 2.41e-53

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: 180.37  E-value: 2.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 585 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 664
Cdd:cd01178   1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                        90       100
                ....*....|....*....|.
gi 27886563 665 YFYVSNGRRKRSPTQSFRFLP 685
Cdd:cd01178  81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 419-578 2.81e-29

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: 114.71  E-value: 2.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   419 LRIEVQPRAH-HRAHYETEG-SRGAVKAA-----PGGHPVVKLLGYSEKPLtLQMFIGTADERnLRPHAfyqvHRITGKM 491
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGEsstrsKKTFPTVQICNYDGPAV-IRVSLVTKDEP-HRPHP----HSLVGKD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   492 vatasyeavvSGTKVLEMTLLPENnMAANIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLVF 554
Cdd:pfam00554  75 ----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCF 143

                         170       180
                  ....*....|....*....|....*.
gi 27886563   555 RVHVP--QGGGKVVSVQAASVPIECS 578
Cdd:pfam00554 144 QAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 587-685 8.90e-23

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: 93.78  E-value: 8.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   587 QVEAYSPSACSVRGGEELVLTGSNFLP-DSKVVFIERGpDGKLQWEEEATVNRLQSNE-VTLTLTVPEYSNKRVSRPVQV 664
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEED-DGQEVWEAEGDFSKTDVHRqVAIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|..
gi 27886563   665 YFYVSNGRRK-RSPTQSFRFLP 685
Cdd:pfam16179  80 NIQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
585-684 6.25e-14

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 68.22  E-value: 6.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563    585 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGpdgklqWEEEATVnrLQSNEVTLTLTVPEYSNKRVSRPVQV 664
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV------GEAPCTF--SPSSSTAIVCKTPPYHNIPGSVPVRT 72

                           90       100
                   ....*....|....*....|
gi 27886563    665 yFYVSNGRRKRSPtQSFRFL 684
Cdd:smart00429  73 -VGLRNGGVPSSP-QPFTYV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 214-413 6.51e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   214 PLPSPRASPRPWTPEDPWSLYGPSPGGRGPEdswlLLSAPGPTPASPRPASPCGKRRYSSSGTPS-SASPALSRRGSLGE 292
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   293 EGSEPPPPPPLPLARDPGSPGPFDYVGAPPAESIPQKTRRTSSEQA-------VALPRSEEPASCNGKLPLGAEESVAPP 365
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptSAQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 27886563   366 GGSRKEVAGMDYLAVPSPLAWSKARIGGHSPIFRTS---ALPPLDWPLPSQ 413
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQPERPPQ 2910
 
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 ...
 407-580 5.69e-125

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: 374.53  E-value: 5.69e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 407 DWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYSE-KPLTLQMFIGTADERNLRPHAFYQVH 485
Cdd:cd07881   1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 486 RITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKV 565
Cdd:cd07881  81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                       170
                ....*....|....*
gi 27886563 566 VSVQAASVPIECSQR 580
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 ...
 418-579 3.50e-65

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: 215.60  E-value: 3.50e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 418 ELRIEVQPRAHHRAHYETEGSRGAVKAAP-GGHPVVKLLGYSEkPLTLQMFIGTADERnLRPHAFYQVHRITGKmVATAS 496
Cdd:cd07927   2 ELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGYME-PVGLQVFIGTASGR-LKPHAFYQVHRITGK-TTTPC 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 497 YEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKVVSVQAASVPIE 576
Cdd:cd07927  79 KEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIE 158


                ...
gi 27886563 577 CSQ 579
Cdd:cd07927 159 CSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 418-579 7.34e-54

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: 184.25  E-value: 7.34e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 418 ELRIEVQPRAHHRAHYETEGSRGAVKAAPG-GHPVVKLLGYSeKPLTLQMFIGTaDERNLRPHAFYQVHRITGKMvATAS 496
Cdd:cd07882   2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGYN-KPVVLQVFVGT-DSGRVKPHGFYQACKVTGRN-TTPC 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 497 YEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKVVSVQAASVPIE 576
Cdd:cd07882  79 EEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPIL 158


                ...
gi 27886563 577 CSQ 579
Cdd:cd07882 159 CTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 585-685 2.41e-53

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: 180.37  E-value: 2.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 585 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 664
Cdd:cd01178   1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                        90       100
                ....*....|....*....|.
gi 27886563 665 YFYVSNGRRKRSPTQSFRFLP 685
Cdd:cd01178  81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 418-579 1.47e-33

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: 127.10  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 418 ELRIEVQPRAH-HRAHYETEG-SRGAVKAA-----PGGHPVVKLLGYSEkPLTLQMFIGTADERnLRPHAfYQVHRITGk 490
Cdd:cd07827   2 YLEITEQPKQRgHRFRYECEGrSAGSIPGEnstadRKTFPTVKLRNYNG-PAKIVVSLVTKDDP-PKPHP-HQLVGKTD- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 491 mvatasyeavvSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETD-----------------IGRKNTRVRLV 553
Cdd:cd07827  78 -----------CRDGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLC 146

                       170       180
                ....*....|....*....|....*...
gi 27886563 554 FRVHVP--QGGGKVVSVQAASVPIECSQ 579
Cdd:cd07827 147 FQAFIEdsDGGFTLPLPPVLSNPIYDKK 174
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 586-685 2.76e-30

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: 115.07  E-value: 2.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 586 PQVEAYSPSACSVRGGEELVLTGSNFL-PDSKVVFIERGPdGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 664
Cdd:cd00602   1 LPICRVSSLSGSVNGGDEVFLLCDKVNkPDIKVWFGEKGP-GETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79

                        90       100
                ....*....|....*....|..
gi 27886563 665 YFYVSNGR-RKRSPTQSFRFLP 685
Cdd:cd00602  80 PIQLVRPDdRKRSEPLTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 419-578 2.81e-29

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: 114.71  E-value: 2.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   419 LRIEVQPRAH-HRAHYETEG-SRGAVKAA-----PGGHPVVKLLGYSEKPLtLQMFIGTADERnLRPHAfyqvHRITGKM 491
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGEsstrsKKTFPTVQICNYDGPAV-IRVSLVTKDEP-HRPHP----HSLVGKD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   492 vatasyeavvSGTKVLEMTLLPENnMAANIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLVF 554
Cdd:pfam00554  75 ----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCF 143

                         170       180
                  ....*....|....*....|....*.
gi 27886563   555 RVHVP--QGGGKVVSVQAASVPIECS 578
Cdd:pfam00554 144 QAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 587-685 8.90e-23

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: 93.78  E-value: 8.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   587 QVEAYSPSACSVRGGEELVLTGSNFLP-DSKVVFIERGpDGKLQWEEEATVNRLQSNE-VTLTLTVPEYSNKRVSRPVQV 664
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEED-DGQEVWEAEGDFSKTDVHRqVAIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|..
gi 27886563   665 YFYVSNGRRK-RSPTQSFRFLP 685
Cdd:pfam16179  80 NIQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
585-684 6.25e-14

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 68.22  E-value: 6.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563    585 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGpdgklqWEEEATVnrLQSNEVTLTLTVPEYSNKRVSRPVQV 664
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV------GEAPCTF--SPSSSTAIVCKTPPYHNIPGSVPVRT 72

                           90       100
                   ....*....|....*....|
gi 27886563    665 yFYVSNGRRKRSPtQSFRFL 684
Cdd:smart00429  73 -VGLRNGGVPSSP-QPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 586-685 6.47e-10

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: 56.70  E-value: 6.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 586 PQVEAYSPSACSVRGGEELVLTGSNFL--PDSKVVFIergpdgklqweEEATVNRLQSNEVTLTLTVPEYSNKrvsRPVQ 663
Cdd:cd00102   1 PVITSISPSSGPVSGGTEVTITGSNFGsgSNLRVTFG-----------GGVPCSVLSVSSTAIVCTTPPYANP---GPGP 66

                        90       100
                ....*....|....*....|...
gi 27886563 664 VYFYVSNGR-RKRSPTQSFRFLP 685
Cdd:cd00102  67 VEVTVDRGNgGITSSPLTFTYVP 89
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 586-683 3.30e-04

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


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 40.12  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   586 PQVEAYSPSACSVRGGEELVLTGSNFLPDSkvvfiergPDGKLQWEEEATVNrLQSNEVTLTLTVPEYSNKRVSRPVQVy 665
Cdd:pfam01833   1 PVITSISPSSGPASGGTTITITGSNFGTDS--------SDLKVTIGGTPCTV-ISVSSTTIVCTTPPGTSGLVNVSVTV- 70

                          90
                  ....*....|....*...
gi 27886563   666 fyvsNGRRKRSPTQSFRF 683
Cdd:pfam01833  71 ----GGGGISSSPLTFTY 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 214-413 6.51e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   214 PLPSPRASPRPWTPEDPWSLYGPSPGGRGPEdswlLLSAPGPTPASPRPASPCGKRRYSSSGTPS-SASPALSRRGSLGE 292
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563   293 EGSEPPPPPPLPLARDPGSPGPFDYVGAPPAESIPQKTRRTSSEQA-------VALPRSEEPASCNGKLPLGAEESVAPP 365
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptSAQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 27886563   366 GGSRKEVAGMDYLAVPSPLAWSKARIGGHSPIFRTS---ALPPLDWPLPSQ 413
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQPERPPQ 2910
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 597-685 3.04e-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: 38.07  E-value: 3.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27886563 597 SVRGGEELVLtgsnfL------PDSKVVFIERGPDGKLqWE-----EEATVNRlqsnEVTLTLTVPEYSNKRVSRPVQVY 665
Cdd:cd01177  12 SVKGGDEVYL-----LcdkvqkEDIQVRFFEEDEEETV-WEafgdfSQTDVHR----QYAIVFRTPPYHDPDITEPVKVK 81

                        90       100
                ....*....|....*....|....
gi 27886563 666 FYVsngRRKRSPTQS----FRFLP 685
Cdd:cd01177  82 IQL---KRPSDGERSesvpFTYVP 102
 
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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