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Conserved domains on  [gi|1907129053|ref|XP_036016919|]
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nuclear factor of activated T-cells, cytoplasmic 1 isoform X1 [Mus musculus]

Protein Classification

RHD-n_NFAT and IPT domain-containing protein( domain architecture ID 10167657)

RHD-n_NFAT and IPT domain-containing protein

Graphical summary

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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 ...
 425-599 6.79e-131

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: 391.10  E-value: 6.79e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 425 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVH 504
Cdd:cd07881     1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 505 RITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRT 584
Cdd:cd07881    81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                         170
                  ....*....|....*
gi 1907129053 585 LSLQVASNPIECSQR 599
Cdd:cd07881   161 LSLQVASNPIECSQR 175
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 604-704 3.47e-44

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


The actual alignment was detected with superfamily member cd01178:

Pssm-ID: 472823  Cd Length: 101  Bit Score: 154.95  E-value: 3.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 604 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 683
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 1907129053 684 SFYVCNGKRKRSQYQRFTYLP 704
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 704-897 1.48e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  704 PANVPIIKTEPTDDFEPALTCGPMS--------QGISP-LPRPYYS------QQLTMPPDPGSCLVAGFAPCSQRNTLM- 767
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPApappaapaAGPPRrLTRPAVAslsesrESLPSPWDPADPPAAVLAPAAALPPAAs 2823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  768 PTPPNASPKLHDLSSPAYTKGLTNPGHSGHLGLQP--PASEAPTmqevPRPMAIQPNSPEQPPSARL-QPQVSPHLNSsc 844
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPP----SRSPAAKPAAPARPPVRRLaRPAVSRSTES-- 2897

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907129053  845 plgrrQVLCPNSPSSPLPSAAQEPACLQSSALPPDMghRQPQPQKVQRNESPA 897
Cdd:PHA03247  2898 -----FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPL 2943
 
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 ...
 425-599 6.79e-131

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: 391.10  E-value: 6.79e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 425 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVH 504
Cdd:cd07881     1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 505 RITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRT 584
Cdd:cd07881    81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                         170
                  ....*....|....*
gi 1907129053 585 LSLQVASNPIECSQR 599
Cdd:cd07881   161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 604-704 3.47e-44

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


Pssm-ID: 238583  Cd Length: 101  Bit Score: 154.95  E-value: 3.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 604 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 683
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 1907129053 684 SFYVCNGKRKRSQYQRFTYLP 704
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 437-597 3.35e-37

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 137.44  E-value: 3.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 437 LRIEVQPKSH-HRAHYETEG-SRGAVKA-----SAGGHPIVQLHGYLEnePLTLQLFIGTADDRLlRPHAfyqvHRITGK 509
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDG--PAVIRVSLVTKDEPH-RPHP----HSLVGK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 510 TvsttsheiilSNTKVLEIPLLPENnMRAIIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLV 572
Cdd:pfam00554  74 D----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142

                         170       180
                  ....*....|....*....|....*..
gi 1907129053 573 FRVHIP--QPNGRTLSLQVASNPIECS 597
Cdd:pfam00554 143 FQAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 607-704 4.39e-28

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 108.80  E-value: 4.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 607 VEKQSTDSYPVIGGKKMVLSGHNFL-QDSKVIFVEKApDGHHVWEMEAKTDRDLCKPNS-LVVEIPPFRNQRITSPVQVS 684
Cdd:pfam16179   2 ICRLSLCSGSVTGGEEIILLCEKVLkDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|.
gi 1907129053 685 FYVCNGKRK-RSQYQRFTYLP 704
Cdd:pfam16179  81 IQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
604-703 1.28e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 61.67  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  604 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFvekapdGHHVWEMEAKTDRDlcKPNSLVVEIPPFRNQRITSPVQV 683
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFV------EVGVGEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRT 72

                           90       100
                   ....*....|....*....|
gi 1907129053  684 sFYVCNGKRkRSQYQRFTYL 703
Cdd:smart00429  73 -VGLRNGGV-PSSPQPFTYV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 704-897 1.48e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  704 PANVPIIKTEPTDDFEPALTCGPMS--------QGISP-LPRPYYS------QQLTMPPDPGSCLVAGFAPCSQRNTLM- 767
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPApappaapaAGPPRrLTRPAVAslsesrESLPSPWDPADPPAAVLAPAAALPPAAs 2823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  768 PTPPNASPKLHDLSSPAYTKGLTNPGHSGHLGLQP--PASEAPTmqevPRPMAIQPNSPEQPPSARL-QPQVSPHLNSsc 844
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPP----SRSPAAKPAAPARPPVRRLaRPAVSRSTES-- 2897

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907129053  845 plgrrQVLCPNSPSSPLPSAAQEPACLQSSALPPDMghRQPQPQKVQRNESPA 897
Cdd:PHA03247  2898 -----FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPL 2943
 
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 ...
 425-599 6.79e-131

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: 391.10  E-value: 6.79e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 425 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVH 504
Cdd:cd07881     1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 505 RITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRT 584
Cdd:cd07881    81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160

                         170
                  ....*....|....*
gi 1907129053 585 LSLQVASNPIECSQR 599
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 ...
 435-598 1.22e-72

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143648  Cd Length: 161  Bit Score: 236.40  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 435 YELRIEVQPKSHHRAHYETEGSRGAVKASA-GGHPIVQLHGYleNEPLTLQLFIGTADDRLlRPHAFYQVHRITGKTvST 513
Cdd:cd07927     1 YELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGY--MEPVGLQVFIGTASGRL-KPHAFYQVHRITGKT-TT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 514 TSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRTLSLQVASNP 593
Cdd:cd07927    77 PCKEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNP 156


                  ....*
gi 1907129053 594 IECSQ 598
Cdd:cd07927   157 IECSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
 436-598 3.79e-58

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


Pssm-ID: 143642  Cd Length: 161  Bit Score: 196.58  E-value: 3.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 436 ELRIEVQPKSHHRAHYETEGSRGAVKASAG-GHPIVQLHGYleNEPLTLQLFIGTADDRLlRPHAFYQVHRITGKTvSTT 514
Cdd:cd07882     2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGY--NKPVVLQVFVGTDSGRV-KPHGFYQACKVTGRN-TTP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 515 SHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRTLSLQVASNPI 594
Cdd:cd07882    78 CEEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157


                  ....
gi 1907129053 595 ECSQ 598
Cdd:cd07882   158 LCTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 604-704 3.47e-44

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


Pssm-ID: 238583  Cd Length: 101  Bit Score: 154.95  E-value: 3.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 604 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 683
Cdd:cd01178     1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80

                          90       100
                  ....*....|....*....|.
gi 1907129053 684 SFYVCNGKRKRSQYQRFTYLP 704
Cdd:cd01178    81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 437-597 3.35e-37

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 137.44  E-value: 3.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 437 LRIEVQPKSH-HRAHYETEG-SRGAVKA-----SAGGHPIVQLHGYLEnePLTLQLFIGTADDRLlRPHAfyqvHRITGK 509
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDG--PAVIRVSLVTKDEPH-RPHP----HSLVGK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 510 TvsttsheiilSNTKVLEIPLLPENnMRAIIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLV 572
Cdd:pfam00554  74 D----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142

                         170       180
                  ....*....|....*....|....*..
gi 1907129053 573 FRVHIP--QPNGRTLSLQVASNPIECS 597
Cdd:pfam00554 143 FQAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 435-598 4.11e-37

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


Pssm-ID: 143640  Cd Length: 174  Bit Score: 137.50  E-value: 4.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 435 YELRIEVQPKSH-HRAHYETEG-SRGAVK-----ASAGGHPIVQLHGYleNEPLTLQLFIGTADDRLlRPHAfYQVHRIT 507
Cdd:cd07827     1 PYLEITEQPKQRgHRFRYECEGrSAGSIPgenstADRKTFPTVKLRNY--NGPAKIVVSLVTKDDPP-KPHP-HQLVGKT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 508 GKTvsttsheiilsnTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETD-----------------IGRKNTRVR 570
Cdd:cd07827    77 DCR------------DGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVR 144

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907129053 571 LVFRVHIPQPNG-RTLSL-QVASNPIECSQ 598
Cdd:cd07827   145 LCFQAFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 607-704 4.39e-28

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 108.80  E-value: 4.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 607 VEKQSTDSYPVIGGKKMVLSGHNFL-QDSKVIFVEKApDGHHVWEMEAKTDRDLCKPNS-LVVEIPPFRNQRITSPVQVS 684
Cdd:pfam16179   2 ICRLSLCSGSVTGGEEIILLCEKVLkDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|.
gi 1907129053 685 FYVCNGKRK-RSQYQRFTYLP 704
Cdd:pfam16179  81 IQLRRPSDKaTSEPQPFTYLP 101
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 605-704 7.67e-26

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 102.36  E-value: 7.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 605 PLVEKQSTDSYPVIGGKKMVLSGHNFL-QDSKVIFVEKAPdGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVQV 683
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNkPDIKVWFGEKGP-GETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79

                          90       100
                  ....*....|....*....|..
gi 1907129053 684 SFYVCNG-KRKRSQYQRFTYLP 704
Cdd:cd00602    80 PIQLVRPdDRKRSEPLTFTYTP 101
IPT smart00429
ig-like, plexins, transcription factors;
604-703 1.28e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 61.67  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  604 LPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFvekapdGHHVWEMEAKTDRDlcKPNSLVVEIPPFRNQRITSPVQV 683
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFV------EVGVGEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPVRT 72

                           90       100
                   ....*....|....*....|
gi 1907129053  684 sFYVCNGKRkRSQYQRFTYL 703
Cdd:smart00429  73 -VGLRNGGV-PSSPQPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 605-704 3.74e-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: 45.92  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 605 PLVEKQSTDSYPVIGGKKMVLSGHNFL--QDSKVIFVEKAPdghhvwemeakTDRDLCKPNSLVVEIPPFRNQritSPVQ 682
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGsgSNLRVTFGGGVP-----------CSVLSVSSTAIVCTTPPYANP---GPGP 66

                          90       100
                  ....*....|....*....|...
gi 1907129053 683 VSFYVCN-GKRKRSQYQRFTYLP 704
Cdd:cd00102    67 VEVTVDRgNGGITSSPLTFTYVP 89
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 434-594 3.87e-06

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator.


Pssm-ID: 143644  Cd Length: 159  Bit Score: 47.81  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 434 PYeLRIEVQPKSHHRAHYETE--GSRGAVKA-----SAGGHPIVQLHGYleNEPLTLQLFIGTADDRLLRPHafyqVHRI 506
Cdd:cd07884     1 PF-LRIVEQPVDKFRFRYKSEmhGTHGSLLGerstsSKKTFPTVKLCNY--RGQAVIRCSLYQADDNRRKPH----VHKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053 507 TGKTVSTTSHEIILSNTKvleipllPENNMRAIIDCAGIL---KLRNSDIELRKGETDIgrknTRVRLVFRVHIPQPNG- 582
Cdd:cd07884    74 VGKQGDDDVCDPHDIEVS-------PEGDYVAMFQNMGIIhtaKKNIPEELYKKKNMNL----NQVVLRFQAFAVSANGh 142

                         170
                  ....*....|...
gi 1907129053 583 -RTLSLQVASNPI 594
Cdd:cd07884   143 lRPICPPVYSNPI 155
PHA03247 PHA03247
large tegument protein UL36; Provisional
 704-897 1.48e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  704 PANVPIIKTEPTDDFEPALTCGPMS--------QGISP-LPRPYYS------QQLTMPPDPGSCLVAGFAPCSQRNTLM- 767
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPApappaapaAGPPRrLTRPAVAslsesrESLPSPWDPADPPAAVLAPAAALPPAAs 2823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129053  768 PTPPNASPKLHDLSSPAYTKGLTNPGHSGHLGLQP--PASEAPTmqevPRPMAIQPNSPEQPPSARL-QPQVSPHLNSsc 844
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPP----SRSPAAKPAAPARPPVRRLaRPAVSRSTES-- 2897

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907129053  845 plgrrQVLCPNSPSSPLPSAAQEPACLQSSALPPDMghRQPQPQKVQRNESPA 897
Cdd:PHA03247  2898 -----FALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPL 2943
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 633-704 2.44e-03

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 38.45  E-value: 2.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907129053 633 DSKVIFVEKAPDGHhVWEMEAK-TDRDLCKPNSLVVEIPPFRNQRITSPVQVSFYVcngKRKRSQYQR----FTYLP 704
Cdd:cd01177    30 DIQVRFFEEDEEET-VWEAFGDfSQTDVHRQYAIVFRTPPYHDPDITEPVKVKIQL---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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