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Conserved domains on  [gi|17136726|ref|NP_476868|]
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suppressor of hairless, isoform A [Drosophila melanogaster]

Protein Classification

RBPJ family protein( domain architecture ID 10558084)

RBPJ family protein similar to the recombining binding protein suppressor of hairless protein, a transcriptional regulator that plays a central role in the Notch signaling pathway involved in cell-cell communication, which regulates a broad spectrum of cell-fate determinations.

CATH:  2.60.40.1450
Gene Ontology:  GO:0001228|GO:0006357
PubMed:  29478922|15288264|19101542|23555033

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BTD pfam09270
Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a ...
 280-402 3.47e-90

Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a beta-trefoil fold, that is, a capped beta-barrel with internal pseudo threefold symmetry. In the DNA-binding protein LAG-1, it also is the site of mutually exclusive interactions with NotchIC (and the viral protein EBNA2) and co-repressors (SMRT/N-Cor and CIR).


:

Pssm-ID: 462734  Cd Length: 123  Bit Score: 273.82  E-value: 3.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   280 ENGHFHASSTQWGAFTIHLLDDNESESEEFQVRDGYIHYGATVKLVCSVTGMALPRLIIRKVDKQMALLEADDPVSQLHK 359
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQENFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDADEPVSQLHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 17136726   360 CAFYMKDTDRMYLCLSQEKIIQFQATPCPKEPNKEMINDGACW 402
Cdd:pfam09270  81 CAFQMKDTERMYLCLSQEKIIQFQATPCPKDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
 122-252 2.63e-69

LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical proteins and in the DNA-binding protein LAG-1. They adopt a beta sandwich structure, with nine strands in two beta-sheets, in a Greek-key topology, and allow for DNA binding. This domain is also known as RHR-N (Rel-homology region) as it related to Rel domain proteins.


:

Pssm-ID: 462735  Cd Length: 148  Bit Score: 220.65  E-value: 2.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   122 IVILHAKVAQKSYGNEKRFFCPPPCIYLFGSGW------RRRYEEMLQQ--------GEGEQGAQLCAFIG-IGS-SDQD 185
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWktkstaLSPDNPLTAPrvtisisgEDSAEESQCIAWIGmIGStSDQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136726   186 MQQLDLNGKQYCAAKTLFISDSD-KRKHFMLSVKMFYGNGHDIGVFNSKRIKVISKPSKKKQSLKNAD 252
Cdd:pfam09271  81 TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQSLKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
 424-520 1.65e-67

IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was initially considered to be involved in V(D)J recombination because of its DNA binding specificity and structural similarity to site-specific recombinases known as the integrase family. Further studies indicated that RBP-J kappa functions as a repressor of transcription, via destabilization of the general transcription factor IID and recruitment of histone deacetylase complexes.


:

Pssm-ID: 238581  Cd Length: 97  Bit Score: 214.24  E-value: 1.65e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726 424 PVTPVPIVNSLNLNGGGDVAMLELSGDNFTPHLQVWFGDVEAETMYRCTETLLCVVPEISQFRGEWLWVRQPTQVPISLV 503
Cdd:cd01176   1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVRQPVQVPISLV 80

                        90
                ....*....|....*..
gi 17136726 504 RNDGIIYATGLTFTYTP 520
Cdd:cd01176  81 RNDGIIYPTGLTFTYTP 97
 
Name Accession Description Interval E-value
BTD pfam09270
Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a ...
 280-402 3.47e-90

Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a beta-trefoil fold, that is, a capped beta-barrel with internal pseudo threefold symmetry. In the DNA-binding protein LAG-1, it also is the site of mutually exclusive interactions with NotchIC (and the viral protein EBNA2) and co-repressors (SMRT/N-Cor and CIR).


Pssm-ID: 462734  Cd Length: 123  Bit Score: 273.82  E-value: 3.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   280 ENGHFHASSTQWGAFTIHLLDDNESESEEFQVRDGYIHYGATVKLVCSVTGMALPRLIIRKVDKQMALLEADDPVSQLHK 359
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQENFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDADEPVSQLHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 17136726   360 CAFYMKDTDRMYLCLSQEKIIQFQATPCPKEPNKEMINDGACW 402
Cdd:pfam09270  81 CAFQMKDTERMYLCLSQEKIIQFQATPCPKDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
 122-252 2.63e-69

LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical proteins and in the DNA-binding protein LAG-1. They adopt a beta sandwich structure, with nine strands in two beta-sheets, in a Greek-key topology, and allow for DNA binding. This domain is also known as RHR-N (Rel-homology region) as it related to Rel domain proteins.


Pssm-ID: 462735  Cd Length: 148  Bit Score: 220.65  E-value: 2.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   122 IVILHAKVAQKSYGNEKRFFCPPPCIYLFGSGW------RRRYEEMLQQ--------GEGEQGAQLCAFIG-IGS-SDQD 185
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWktkstaLSPDNPLTAPrvtisisgEDSAEESQCIAWIGmIGStSDQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136726   186 MQQLDLNGKQYCAAKTLFISDSD-KRKHFMLSVKMFYGNGHDIGVFNSKRIKVISKPSKKKQSLKNAD 252
Cdd:pfam09271  81 TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQSLKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
 424-520 1.65e-67

IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was initially considered to be involved in V(D)J recombination because of its DNA binding specificity and structural similarity to site-specific recombinases known as the integrase family. Further studies indicated that RBP-J kappa functions as a repressor of transcription, via destabilization of the general transcription factor IID and recruitment of histone deacetylase complexes.


Pssm-ID: 238581  Cd Length: 97  Bit Score: 214.24  E-value: 1.65e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726 424 PVTPVPIVNSLNLNGGGDVAMLELSGDNFTPHLQVWFGDVEAETMYRCTETLLCVVPEISQFRGEWLWVRQPTQVPISLV 503
Cdd:cd01176   1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVRQPVQVPISLV 80

                        90
                ....*....|....*..
gi 17136726 504 RNDGIIYATGLTFTYTP 520
Cdd:cd01176  81 RNDGIIYPTGLTFTYTP 97
TIG_SUH pfam20144
TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless ...
 429-518 4.32e-44

TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless protein.


Pssm-ID: 466305  Cd Length: 92  Bit Score: 151.98  E-value: 4.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   429 PIVNSLNLNGGGDVAMLELSGDNFTPHLQVWFGDVEAETMYRCTETLLCVVPEISQFRGEWLW--VRQPTQVPISLVRND 506
Cdd:pfam20144   1 PVVSSLTVNGGGENAMLELHGENFTRDLKVWFGDIKAETEYRSRESLVCVVPDASELLSSWTSqkDRKKKKVPLLLVRGD 80

                          90
                  ....*....|..
gi 17136726   507 GIIYATGLTFTY 518
Cdd:pfam20144  81 GVIYKTGLTFTY 92
 
Name Accession Description Interval E-value
BTD pfam09270
Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a ...
 280-402 3.47e-90

Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a beta-trefoil fold, that is, a capped beta-barrel with internal pseudo threefold symmetry. In the DNA-binding protein LAG-1, it also is the site of mutually exclusive interactions with NotchIC (and the viral protein EBNA2) and co-repressors (SMRT/N-Cor and CIR).


Pssm-ID: 462734  Cd Length: 123  Bit Score: 273.82  E-value: 3.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   280 ENGHFHASSTQWGAFTIHLLDDNESESEEFQVRDGYIHYGATVKLVCSVTGMALPRLIIRKVDKQMALLEADDPVSQLHK 359
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQENFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDADEPVSQLHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 17136726   360 CAFYMKDTDRMYLCLSQEKIIQFQATPCPKEPNKEMINDGACW 402
Cdd:pfam09270  81 CAFQMKDTERMYLCLSQEKIIQFQATPCPKDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
 122-252 2.63e-69

LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical proteins and in the DNA-binding protein LAG-1. They adopt a beta sandwich structure, with nine strands in two beta-sheets, in a Greek-key topology, and allow for DNA binding. This domain is also known as RHR-N (Rel-homology region) as it related to Rel domain proteins.


Pssm-ID: 462735  Cd Length: 148  Bit Score: 220.65  E-value: 2.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   122 IVILHAKVAQKSYGNEKRFFCPPPCIYLFGSGW------RRRYEEMLQQ--------GEGEQGAQLCAFIG-IGS-SDQD 185
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWktkstaLSPDNPLTAPrvtisisgEDSAEESQCIAWIGmIGStSDQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136726   186 MQQLDLNGKQYCAAKTLFISDSD-KRKHFMLSVKMFYGNGHDIGVFNSKRIKVISKPSKKKQSLKNAD 252
Cdd:pfam09271  81 TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQSLKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
 424-520 1.65e-67

IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was initially considered to be involved in V(D)J recombination because of its DNA binding specificity and structural similarity to site-specific recombinases known as the integrase family. Further studies indicated that RBP-J kappa functions as a repressor of transcription, via destabilization of the general transcription factor IID and recruitment of histone deacetylase complexes.


Pssm-ID: 238581  Cd Length: 97  Bit Score: 214.24  E-value: 1.65e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726 424 PVTPVPIVNSLNLNGGGDVAMLELSGDNFTPHLQVWFGDVEAETMYRCTETLLCVVPEISQFRGEWLWVRQPTQVPISLV 503
Cdd:cd01176   1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVRQPVQVPISLV 80

                        90
                ....*....|....*..
gi 17136726 504 RNDGIIYATGLTFTYTP 520
Cdd:cd01176  81 RNDGIIYPTGLTFTYTP 97
TIG_SUH pfam20144
TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless ...
 429-518 4.32e-44

TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless protein.


Pssm-ID: 466305  Cd Length: 92  Bit Score: 151.98  E-value: 4.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726   429 PIVNSLNLNGGGDVAMLELSGDNFTPHLQVWFGDVEAETMYRCTETLLCVVPEISQFRGEWLW--VRQPTQVPISLVRND 506
Cdd:pfam20144   1 PVVSSLTVNGGGENAMLELHGENFTRDLKVWFGDIKAETEYRSRESLVCVVPDASELLSSWTSqkDRKKKKVPLLLVRGD 80

                          90
                  ....*....|..
gi 17136726   507 GIIYATGLTFTY 518
Cdd:pfam20144  81 GVIYKTGLTFTY 92
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 426-520 1.62e-30

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 115.07  E-value: 1.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726 426 TPVPIVNSLNLNG-GGDVAMLELSGDNFtPHLQVWFGD-------VEAETMYRCTE-TLLCVVPEISQFRGEWlwVRQPT 496
Cdd:cd00602   1 LPICRVSSLSGSVnGGDEVFLLCDKVNK-PDIKVWFGEkgpgetvWEAEAMFRQEDvRQVAIVFKTPPYHNKW--ITRPV 77

                        90       100
                ....*....|....*....|....
gi 17136726 497 QVPISLVRNDGIIYATGLTFTYTP 520
Cdd:cd00602  78 QVPIQLVRPDDRKRSEPLTFTYTP 101
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 439-520 5.75e-09

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: 53.23  E-value: 5.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136726 439 GGDVAMLELSGDNFTPHLQVWF-GDVEAETMYRCTETLLCVVPEISQfrgewlwvRQPTQVPISLVRNDGIIYATGLTFT 517
Cdd:cd00102  15 GGTEVTITGSNFGSGSNLRVTFgGGVPCSVLSVSSTAIVCTTPPYAN--------PGPGPVEVTVDRGNGGITSSPLTFT 86


                ...
gi 17136726 518 YTP 520
Cdd:cd00102  87 YVP 89
 
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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