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Conserved domains on  [gi|27502386|ref|NP_765975|]
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nuclear factor of activated T-cells, cytoplasmic 1 isoform C [Homo sapiens]

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 ...
403-577 7.78e-129

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: 385.32  E-value: 7.78e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 403 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVH 482
Cdd:cd07881   1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 483 RITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRT 562
Cdd:cd07881  81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                       170
                ....*....|....*
gi 27502386 563 LSLQVASNPIECSQR 577
Cdd:cd07881 161 LSLQVASNPIECSQR 175
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
582-682 2.17e-43

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: 152.64  E-value: 2.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 582 LPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHV 661
Cdd:cd01178   1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80
                        90       100
                ....*....|....*....|.
gi 27502386 662 SFYVCNGKRKRSQYQRFTYLP 682
Cdd:cd01178  81 QFYVVNGKRKRSQPQTFTYTP 101
PHA03247 super family cl33720
large tegument protein UL36; Provisional
699-877 1.11e-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: 43.00  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   699 APTCGPVSQGLSPLPRPYYSqqLAMPPDPssclvaGFPPCPQRSTLMPAAPgvspklhdLSPAAYTKGVASPGHCHLGLP 778
Cdd:PHA03247 2678 SPPQRPRRRAARPTVGSLTS--LADPPPP------PPTPEPAPHALVSATP--------LPPGPAAARQASPALPAAPAP 2741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   779 QPAGEAPAVQDVPRPVA-----------THPGSPGQPPPALLPQQVSAPPSSSCPPGLEHSLCPSSPSPPLPPATQEPTC 847
Cdd:PHA03247 2742 PAVPAGPATPGGPARPArppttagppapAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821
                         170       180       190
                  ....*....|....*....|....*....|
gi 27502386   848 LQPCSPACPPATGRPQHLPSTVRRDESPTA 877
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
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 ...
403-577 7.78e-129

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: 385.32  E-value: 7.78e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 403 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVH 482
Cdd:cd07881   1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 483 RITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRT 562
Cdd:cd07881  81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                       170
                ....*....|....*
gi 27502386 563 LSLQVASNPIECSQR 577
Cdd:cd07881 161 LSLQVASNPIECSQR 175
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
582-682 2.17e-43

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: 152.64  E-value: 2.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 582 LPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHV 661
Cdd:cd01178   1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80
                        90       100
                ....*....|....*....|.
gi 27502386 662 SFYVCNGKRKRSQYQRFTYLP 682
Cdd:cd01178  81 QFYVVNGKRKRSQPQTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
415-575 2.78e-36

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: 134.74  E-value: 2.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   415 LRIEVQPKSH-HRAHYETEG-SRGAVKA-----SAGGHPIVQLHGYLEnePLMLQLFIGTADDRLlRPHAfyqvHRITGK 487
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDG--PAVIRVSLVTKDEPH-RPHP----HSLVGK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   488 TvsttsheailSNTKVLEIPLLPENsMRAVIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLV 550
Cdd:pfam00554  74 D----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142
                         170       180
                  ....*....|....*....|....*..
gi 27502386   551 FRVHVP--QPSGRTLSLQVASNPIECS 575
Cdd:pfam00554 143 FQAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
585-682 6.17e-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: 108.42  E-value: 6.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   585 VEKQSTDSYPVVGGKKMVLSGHNFL-QDSKVIFVEKApDGHHVWEMEAKTDRDLCKPNS-LVVEIPPFRNQRITSPVHVS 662
Cdd:pfam16179   2 ICRLSLCSGSVTGGEEIILLCEKVLkDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|.
gi 27502386   663 FYVCNGKRK-RSQYQRFTYLP 682
Cdd:pfam16179  81 IQLRRPSDKaTSEPQPFTYLP 101
IPT smart00429
ig-like, plexins, transcription factors;
582-681 2.37e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 60.90  E-value: 2.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386    582 LPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFvekapdGHHVWEMEAKTDRDlcKPNSLVVEIPPFRNQRITSPVhV 661
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFV------EVGVGEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPV-R 71
                           90       100
                   ....*....|....*....|
gi 27502386    662 SFYVCNGKRkRSQYQRFTYL 681
Cdd:smart00429  72 TVGLRNGGV-PSSPQPFTYV 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
699-877 1.11e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   699 APTCGPVSQGLSPLPRPYYSqqLAMPPDPssclvaGFPPCPQRSTLMPAAPgvspklhdLSPAAYTKGVASPGHCHLGLP 778
Cdd:PHA03247 2678 SPPQRPRRRAARPTVGSLTS--LADPPPP------PPTPEPAPHALVSATP--------LPPGPAAARQASPALPAAPAP 2741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   779 QPAGEAPAVQDVPRPVA-----------THPGSPGQPPPALLPQQVSAPPSSSCPPGLEHSLCPSSPSPPLPPATQEPTC 847
Cdd:PHA03247 2742 PAVPAGPATPGGPARPArppttagppapAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821
                         170       180       190
                  ....*....|....*....|....*....|
gi 27502386   848 LQPCSPACPPATGRPQHLPSTVRRDESPTA 877
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
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 ...
403-577 7.78e-129

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: 385.32  E-value: 7.78e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 403 DWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVH 482
Cdd:cd07881   1 DWPLPSQSGQYELRIEVQPKPHHRAHYETEGSRGAVKASTGGHPVVQLHGYMENKPLTLQMFIGTADDRYLRPHAFYQVH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 483 RITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRT 562
Cdd:cd07881  81 RITGKTVATASQEIIISNTKVLEIPLLPENNMRASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGRV 160
                       170
                ....*....|....*
gi 27502386 563 LSLQVASNPIECSQR 577
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 ...
413-576 5.22e-71

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: 231.78  E-value: 5.22e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 413 YELRIEVQPKSHHRAHYETEGSRGAVKASA-GGHPIVQLHGYleNEPLMLQLFIGTADDRLlRPHAFYQVHRITGKTvST 491
Cdd:cd07927   1 YELRIEVQPEPHHRARYETEGSRGAVKAPStGGFPTVKLHGY--MEPVGLQVFIGTASGRL-KPHAFYQVHRITGKT-TT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 492 TSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNP 571
Cdd:cd07927  77 PCKEKIIGNTKVLEIPLEPKNNMTATIDCAGILKLRNADIELRKGETDIKKKNTRARLVFRVHIPEKDGRIVSLQTASNP 156

                ....*
gi 27502386 572 IECSQ 576
Cdd:cd07927 157 IECSQ 161
RHD-n_TonEBP cd07882
N-terminal sub-domain of the Rel homology domain (RHD) of tonicity-responsive enhancer binding ...
414-576 5.32e-57

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: 193.11  E-value: 5.32e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 414 ELRIEVQPKSHHRAHYETEGSRGAVKASAG-GHPIVQLHGYleNEPLMLQLFIGTADDRLlRPHAFYQVHRITGKTvSTT 492
Cdd:cd07882   2 ELKILVQPETQHRARYLTEGSRGSVKDRSQqGFPTVKLEGY--NKPVVLQVFVGTDSGRV-KPHGFYQACKVTGRN-TTP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 493 SHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPI 572
Cdd:cd07882  78 CEEVDVEGTTVIEVPLDPTNNMTISVDCVGILKLRNADVEARIGIARSKKKSTRVRLVFRVIIPRKDGSTLTLQTVSNPI 157

                ....
gi 27502386 573 ECSQ 576
Cdd:cd07882 158 LCTQ 161
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
582-682 2.17e-43

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: 152.64  E-value: 2.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 582 LPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHV 661
Cdd:cd01178   1 LPEIEKKSLNSCSVNGGEELFLTGKNFLKDSKVVFQEKGQDGEAQWEAEATIDKEKSHQNHLVVEVPPYHNKHVAAPVQV 80
                        90       100
                ....*....|....*....|.
gi 27502386 662 SFYVCNGKRKRSQYQRFTYLP 682
Cdd:cd01178  81 QFYVVNGKRKRSQPQTFTYTP 101
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
413-576 9.98e-37

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


Pssm-ID: 143640  Cd Length: 174  Bit Score: 136.34  E-value: 9.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 413 YELRIEVQPKSH-HRAHYETEG-SRGAVK-----ASAGGHPIVQLHGYleNEPLMLQLFIGTADDRLlRPHAfYQVHRIT 485
Cdd:cd07827   1 PYLEITEQPKQRgHRFRYECEGrSAGSIPgenstADRKTFPTVKLRNY--NGPAKIVVSLVTKDDPP-KPHP-HQLVGKT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 486 GKTvsttsheailsnTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETD-----------------IGRKNTRVR 548
Cdd:cd07827  77 DCR------------DGVCEVRLGPKNNMTASFNNLGIQCVRKKDVEEALGQRIqlgidpfmvhkgpegnaSDIDLNRVR 144
                       170       180       190
                ....*....|....*....|....*....|
gi 27502386 549 LVFRVHVPQPSG-RTLSL-QVASNPIECSQ 576
Cdd:cd07827 145 LCFQAFIEDSDGgFTLPLpPVLSNPIYDKK 174
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
415-575 2.78e-36

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: 134.74  E-value: 2.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   415 LRIEVQPKSH-HRAHYETEG-SRGAVKA-----SAGGHPIVQLHGYLEnePLMLQLFIGTADDRLlRPHAfyqvHRITGK 487
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCEGrSAGSIPGesstrSKKTFPTVQICNYDG--PAVIRVSLVTKDEPH-RPHP----HSLVGK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   488 TvsttsheailSNTKVLEIPLLPENsMRAVIDCAGILKLRNSDIELRKGE---TDIGRKN--------------TRVRLV 550
Cdd:pfam00554  74 D----------CKDGVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKErieLNIDPFNvgfealrqikdmdlNVVRLC 142
                         170       180
                  ....*....|....*....|....*..
gi 27502386   551 FRVHVP--QPSGRTLSLQVASNPIECS 575
Cdd:pfam00554 143 FQAFLPdtRGNFTTPLPPVVSNPIYDK 169
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
585-682 6.17e-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: 108.42  E-value: 6.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   585 VEKQSTDSYPVVGGKKMVLSGHNFL-QDSKVIFVEKApDGHHVWEMEAKTDRDLCKPNS-LVVEIPPFRNQRITSPVHVS 662
Cdd:pfam16179   2 ICRLSLCSGSVTGGEEIILLCEKVLkDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVaIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|.
gi 27502386   663 FYVCNGKRK-RSQYQRFTYLP 682
Cdd:pfam16179  81 IQLRRPSDKaTSEPQPFTYLP 101
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
583-682 9.23e-25

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: 99.28  E-value: 9.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 583 PLVEKQSTDSYPVVGGKKMVLSGHNFL-QDSKVIFVEKAPdGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHV 661
Cdd:cd00602   1 LPICRVSSLSGSVNGGDEVFLLCDKVNkPDIKVWFGEKGP-GETVWEAEAMFRQEDVRQVAIVFKTPPYHNKWITRPVQV 79
                        90       100
                ....*....|....*....|..
gi 27502386 662 SFYVCNG-KRKRSQYQRFTYLP 682
Cdd:cd00602  80 PIQLVRPdDRKRSEPLTFTYTP 101
IPT smart00429
ig-like, plexins, transcription factors;
582-681 2.37e-11

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 60.90  E-value: 2.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386    582 LPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFvekapdGHHVWEMEAKTDRDlcKPNSLVVEIPPFRNQRITSPVhV 661
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEITLCGKNLKSISVVFV------EVGVGEAPCTFSPS--SSTAIVCKTPPYHNIPGSVPV-R 71
                           90       100
                   ....*....|....*....|
gi 27502386    662 SFYVCNGKRkRSQYQRFTYL 681
Cdd:smart00429  72 TVGLRNGGV-PSSPQPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
583-682 7.27e-06

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


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 45.14  E-value: 7.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 583 PLVEKQSTDSYPVVGGKKMVLSGHNFL--QDSKVIFVEKAPdghhvwemeakTDRDLCKPNSLVVEIPPFRNQRITsPVH 660
Cdd:cd00102   1 PVITSISPSSGPVSGGTEVTITGSNFGsgSNLRVTFGGGVP-----------CSVLSVSSTAIVCTTPPYANPGPG-PVE 68
                        90       100
                ....*....|....*....|..
gi 27502386 661 VSFYVCNGkRKRSQYQRFTYLP 682
Cdd:cd00102  69 VTVDRGNG-GITSSPLTFTYVP 89
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
412-572 1.63e-05

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: 45.88  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 412 PYeLRIEVQPKSHHRAHYETE--GSRGAVKA-----SAGGHPIVQLHGYleNEPLMLQLFIGTADDRLLRPHafyqVHRI 484
Cdd:cd07884   1 PF-LRIVEQPVDKFRFRYKSEmhGTHGSLLGerstsSKKTFPTVKLCNY--RGQAVIRCSLYQADDNRRKPH----VHKL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386 485 TGKTVSTTSHEAILSNTKvleipllPENSMRAVIDCAGIL---KLRNSDIELRKGETDIgrknTRVRLVFRVHVPQPSG- 560
Cdd:cd07884  74 VGKQGDDDVCDPHDIEVS-------PEGDYVAMFQNMGIIhtaKKNIPEELYKKKNMNL----NQVVLRFQAFAVSANGh 142
                       170
                ....*....|...
gi 27502386 561 -RTLSLQVASNPI 572
Cdd:cd07884 143 lRPICPPVYSNPI 155
PHA03247 PHA03247
large tegument protein UL36; Provisional
699-877 1.11e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   699 APTCGPVSQGLSPLPRPYYSqqLAMPPDPssclvaGFPPCPQRSTLMPAAPgvspklhdLSPAAYTKGVASPGHCHLGLP 778
Cdd:PHA03247 2678 SPPQRPRRRAARPTVGSLTS--LADPPPP------PPTPEPAPHALVSATP--------LPPGPAAARQASPALPAAPAP 2741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27502386   779 QPAGEAPAVQDVPRPVA-----------THPGSPGQPPPALLPQQVSAPPSSSCPPGLEHSLCPSSPSPPLPPATQEPTC 847
Cdd:PHA03247 2742 PAVPAGPATPGGPARPArppttagppapAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821
                         170       180       190
                  ....*....|....*....|....*....|
gi 27502386   848 LQPCSPACPPATGRPQHLPSTVRRDESPTA 877
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
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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