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Conserved domains on  [gi|312176395|ref|NP_001185895|]
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nuclear factor of activated T-cells, cytoplasmic 4 isoform 4 [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 ...
 337-510 3.68e-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: 372.99  E-value: 3.68e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 337 DWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYSE-KPLTLQMFIGTADERNLRPHAFYQVH 415
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 416 RITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKV 495
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                        170
                 ....*....|....*
gi 312176395 496 VSVQAASVPIECSQR 510
Cdd:cd07881  161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 515-615 3.23e-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: 179.60  E-value: 3.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 515 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 594
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                         90       100
                 ....*....|....*....|.
gi 312176395 595 YFYVSNGRRKRSPTQSFRFLP 615
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 144-343 5.32e-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: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  144 PLPSPRASPRPWTPEDPWSLYGPSPGGRGPEdswlLLSAPGPTPASPRPASPCGKRRYSSSGTPS-SASPALSRRGSLGE 222
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  223 EGSEPPPPPPLPLARDPGSPGPFDYVGAPPAESIPQKTRRTSSEQA-------VALPRSEEPASCNGKLPLGAEESVAPP 295
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptSAQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312176395  296 GGSRKEVAGMDYLAVPSPLAWSKARIGGHSPIFRTS---ALPPLDWPLPSQ 343
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 ...
 337-510 3.68e-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: 372.99  E-value: 3.68e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 337 DWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYSE-KPLTLQMFIGTADERNLRPHAFYQVH 415
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 416 RITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKV 495
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                        170
                 ....*....|....*
gi 312176395 496 VSVQAASVPIECSQR 510
Cdd:cd07881  161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 515-615 3.23e-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: 179.60  E-value: 3.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 515 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 594
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                         90       100
                 ....*....|....*....|.
gi 312176395 595 YFYVSNGRRKRSPTQSFRFLP 615
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 349-508 3.04e-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: 114.32  E-value: 3.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  349 LRIEVQPRAH-HRAHYETEG-SRGAVKAA-----PGGHPVVKLLGYSEKPLtLQMFIGTADERnLRPHAfyqvHRITGKM 421
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGEsstrsKKTFPTVQICNYDGPAV-IRVSLVTKDEP-HRPHP----HSLVGKD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  422 vatasyeavvSGTKVLEMTLLPENnMAANIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLVF 484
Cdd:pfam00554  75 ----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCF 143

                         170       180
                  ....*....|....*....|....*.
gi 312176395  485 RVHVP--QGGGKVVSVQAASVPIECS 508
Cdd:pfam00554 144 QAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 517-615 9.27e-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: 93.40  E-value: 9.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  517 QVEAYSPSACSVRGGEELVLTGSNFLP-DSKVVFIERGpDGKLQWEEEATVNRLQSNE-VTLTLTVPEYSNKRVSRPVQV 594
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEED-DGQEVWEAEGDFSKTDVHRqVAIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|..
gi 312176395  595 YFYVSNGRRK-RSPTQSFRFLP 615
Cdd:pfam16179  80 NIQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
515-614 8.64e-14

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 8.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395   515 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGpdgklqWEEEATVnrLQSNEVTLTLTVPEYSNKRVSRPVQV 594
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV------GEAPCTF--SPSSSTAIVCKTPPYHNIPGSVPVRT 72

                           90       100
                   ....*....|....*....|
gi 312176395   595 yFYVSNGRRKRSPtQSFRFL 614
Cdd:smart00429  73 -VGLRNGGVPSSP-QPFTYV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 144-343 5.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  144 PLPSPRASPRPWTPEDPWSLYGPSPGGRGPEdswlLLSAPGPTPASPRPASPCGKRRYSSSGTPS-SASPALSRRGSLGE 222
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  223 EGSEPPPPPPLPLARDPGSPGPFDYVGAPPAESIPQKTRRTSSEQA-------VALPRSEEPASCNGKLPLGAEESVAPP 295
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptSAQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312176395  296 GGSRKEVAGMDYLAVPSPLAWSKARIGGHSPIFRTS---ALPPLDWPLPSQ 343
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 ...
 337-510 3.68e-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: 372.99  E-value: 3.68e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 337 DWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYSE-KPLTLQMFIGTADERNLRPHAFYQVH 415
Cdd:cd07881    1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMEnKPLTLQMFIGTADDRYLRPHAFYQVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 416 RITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKV 495
Cdd:cd07881   81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                        170
                 ....*....|....*
gi 312176395 496 VSVQAASVPIECSQR 510
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 ...
 348-509 2.95e-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: 214.83  E-value: 2.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 348 ELRIEVQPRAHHRAHYETEGSRGAVKAAP-GGHPVVKLLGYSEkPLTLQMFIGTADERnLRPHAFYQVHRITGKmVATAS 426
Cdd:cd07927    2 ELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGYME-PVGLQVFIGTASGR-LKPHAFYQVHRITGK-TTTPC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 427 YEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKVVSVQAASVPIE 506
Cdd:cd07927   79 KEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNPIE 158


                 ...
gi 312176395 507 CSQ 509
Cdd:cd07927  159 CSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 348-509 6.95e-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: 183.87  E-value: 6.95e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 348 ELRIEVQPRAHHRAHYETEGSRGAVKAAPG-GHPVVKLLGYSeKPLTLQMFIGTaDERNLRPHAFYQVHRITGKMvATAS 426
Cdd:cd07882    2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGYN-KPVVLQVFVGT-DSGRVKPHGFYQACKVTGRN-TTPC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 427 YEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKVVSVQAASVPIE 506
Cdd:cd07882   79 EEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPIL 158


                 ...
gi 312176395 507 CSQ 509
Cdd:cd07882  159 CTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 515-615 3.23e-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: 179.60  E-value: 3.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 515 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 594
Cdd:cd01178    1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                         90       100
                 ....*....|....*....|.
gi 312176395 595 YFYVSNGRRKRSPTQSFRFLP 615
Cdd:cd01178   81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 348-509 2.20e-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: 126.33  E-value: 2.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 348 ELRIEVQPRAH-HRAHYETEG-SRGAVKAA-----PGGHPVVKLLGYSEkPLTLQMFIGTADERnLRPHAfYQVHRITGk 420
Cdd:cd07827    2 YLEITEQPKQRgHRFRYECEGrSAGSIPGEnstadRKTFPTVKLRNYNG-PAKIVVSLVTKDDP-PKPHP-HQLVGKTD- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 421 mvatasyeavvSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETD-----------------IGRKNTRVRLV 483
Cdd:cd07827   78 -----------CRDGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVRLC 146

                        170       180
                 ....*....|....*....|....*...
gi 312176395 484 FRVHVP--QGGGKVVSVQAASVPIECSQ 509
Cdd:cd07827  147 FQAFIEdsDGGFTLPLPPVLSNPIYDKK 174
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 516-615 3.63e-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: 114.69  E-value: 3.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 516 PQVEAYSPSACSVRGGEELVLTGSNFL-PDSKVVFIERGPdGKLQWEEEATVNRLQSNEVTLTLTVPEYSNKRVSRPVQV 594
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNkPDIKVWFGEKGP-GETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79

                         90       100
                 ....*....|....*....|..
gi 312176395 595 YFYVSNGR-RKRSPTQSFRFLP 615
Cdd:cd00602   80 PIQLVRPDdRKRSEPLTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 349-508 3.04e-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: 114.32  E-value: 3.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  349 LRIEVQPRAH-HRAHYETEG-SRGAVKAA-----PGGHPVVKLLGYSEKPLtLQMFIGTADERnLRPHAfyqvHRITGKM 421
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGEsstrsKKTFPTVQICNYDGPAV-IRVSLVTKDEP-HRPHP----HSLVGKD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  422 vatasyeavvSGTKVLEMTLLPENnMAANIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLVF 484
Cdd:pfam00554  75 ----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLCF 143

                         170       180
                  ....*....|....*....|....*.
gi 312176395  485 RVHVP--QGGGKVVSVQAASVPIECS 508
Cdd:pfam00554 144 QAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 517-615 9.27e-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: 93.40  E-value: 9.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  517 QVEAYSPSACSVRGGEELVLTGSNFLP-DSKVVFIERGpDGKLQWEEEATVNRLQSNE-VTLTLTVPEYSNKRVSRPVQV 594
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKdDIKVRFYEED-DGQEVWEAEGDFSKTDVHRqVAIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|..
gi 312176395  595 YFYVSNGRRK-RSPTQSFRFLP 615
Cdd:pfam16179  80 NIQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
515-614 8.64e-14

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 8.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395   515 LPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGpdgklqWEEEATVnrLQSNEVTLTLTVPEYSNKRVSRPVQV 594
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFVEVGV------GEAPCTF--SPSSSTAIVCKTPPYHNIPGSVPVRT 72

                           90       100
                   ....*....|....*....|
gi 312176395   595 yFYVSNGRRKRSPtQSFRFL 614
Cdd:smart00429  73 -VGLRNGGVPSSP-QPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 516-615 9.69e-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: 55.93  E-value: 9.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 516 PQVEAYSPSACSVRGGEELVLTGSNFL--PDSKVVFIergpdgklqweEEATVNRLQSNEVTLTLTVPEYSNKrvsRPVQ 593
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGsgSNLRVTFG-----------GGVPCSVLSVSSTAIVCTTPPYANP---GPGP 66

                         90       100
                 ....*....|....*....|...
gi 312176395 594 VYFYVSNGR-RKRSPTQSFRFLP 615
Cdd:cd00102   67 VEVTVDRGNgGITSSPLTFTYVP 89
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 516-613 4.36e-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: 39.74  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  516 PQVEAYSPSACSVRGGEELVLTGSNFLPDSkvvfiergPDGKLQWEEEATVNrLQSNEVTLTLTVPEYSNKRVSRPVQVy 595
Cdd:pfam01833   1 PVITSISPSSGPASGGTTITITGSNFGTDS--------SDLKVTIGGTPCTV-ISVSSTTIVCTTPPGTSGLVNVSVTV- 70

                          90
                  ....*....|....*...
gi 312176395  596 fyvsNGRRKRSPTQSFRF 613
Cdd:pfam01833  71 ----GGGGISSSPLTFTY 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 144-343 5.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  144 PLPSPRASPRPWTPEDPWSLYGPSPGGRGPEdswlLLSAPGPTPASPRPASPCGKRRYSSSGTPS-SASPALSRRGSLGE 222
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPA----LPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395  223 EGSEPPPPPPLPLARDPGSPGPFDYVGAPPAESIPQKTRRTSSEQA-------VALPRSEEPASCNGKLPLGAEESVAPP 295
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptSAQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312176395  296 GGSRKEVAGMDYLAVPSPLAWSKARIGGHSPIFRTS---ALPPLDWPLPSQ 343
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfALPPDQPERPPQ 2910
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 527-615 2.80e-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: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176395 527 SVRGGEELVLtgsnfL------PDSKVVFIERGPDGKLqWE-----EEATVNRlqsnEVTLTLTVPEYSNKRVSRPVQVY 595
Cdd:cd01177   12 SVKGGDEVYL-----LcdkvqkEDIQVRFFEEDEEETV-WEafgdfSQTDVHR----QYAIVFRTPPYHDPDITEPVKVK 81

                         90       100
                 ....*....|....*....|....
gi 312176395 596 FYVsngRRKRSPTQS----FRFLP 615
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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