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Conserved domains on  [gi|1831513092|ref|NP_001368385|]
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Suppressor of hairless protein homolog [Caenorhabditis elegans]

Protein Classification

LAG1-DNAbind and BTD domain-containing protein( domain architecture ID 10558086)

protein containing domains LAG1-DNAbind, BTD, and IPT

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 ...
365-490 4.46e-77

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: 240.69  E-value: 4.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 365 EGNAFHASSTKWGAFTIHLFDDERGLQEtdNFAVRDGFVYYGSVVKLVDSVTGIALPRLRIRKVDKQQVILDAscsEEPV 444
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQE--NFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDA---DEPV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831513092 445 SQLHKCAFQMIDNELVYLCLSHDKIIQHQATAI--NEHRHQINDGAAW 490
Cdd:pfam09270  76 SQLHKCAFQMKDTERMYLCLSQEKIIQFQATPCpkDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
171-334 1.02e-64

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: 209.48  E-value: 1.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 171 ISIFHAKVAQKSYGNEKRFFCPPPCIYLIGQGWKLKKdrvaQLYKTLKASAQKDAAIENDPIHEQQATELVAYIGIGSDT 250
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWKTKS----TALSPDNPLTAPRVTISISGEDSAEESQCIAWIGMIGST 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 251 SERQqldfstgkvrhpgDQRQDPNIYDYCAAKTLYISDSD-KRKYFDLNAQFFYGCGMEIGGFVSQRIKVISKPSKKKQS 329
Cdd:pfam09271  77 SDQE-------------TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQS 143

                  ....*
gi 1831513092 330 MKNTD 334
Cdd:pfam09271 144 LKNAD 148
IPT super family cl15674
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
512-614 7.99e-55

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 cd01176:

Pssm-ID: 472823  Cd Length: 97  Bit Score: 181.50  E-value: 7.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 512 PISPCPVVGSLEVDGHGEASRVELHGRDFKPNLKVWFGATPVETTFRSEESLHCSIPPVSQVRNEQTHwmftnrTTGDVE 591
Cdd:cd01176     1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRW------VRQPVQ 74
                          90       100
                  ....*....|....*....|...
gi 1831513092 592 VPISLVRDDGVVYSSGLTFSYKS 614
Cdd:cd01176    75 VPISLVRNDGIIYPTGLTFTYTP 97
 
Name Accession Description Interval E-value
BTD pfam09270
Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a ...
365-490 4.46e-77

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: 240.69  E-value: 4.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 365 EGNAFHASSTKWGAFTIHLFDDERGLQEtdNFAVRDGFVYYGSVVKLVDSVTGIALPRLRIRKVDKQQVILDAscsEEPV 444
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQE--NFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDA---DEPV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831513092 445 SQLHKCAFQMIDNELVYLCLSHDKIIQHQATAI--NEHRHQINDGAAW 490
Cdd:pfam09270  76 SQLHKCAFQMKDTERMYLCLSQEKIIQFQATPCpkDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
171-334 1.02e-64

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: 209.48  E-value: 1.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 171 ISIFHAKVAQKSYGNEKRFFCPPPCIYLIGQGWKLKKdrvaQLYKTLKASAQKDAAIENDPIHEQQATELVAYIGIGSDT 250
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWKTKS----TALSPDNPLTAPRVTISISGEDSAEESQCIAWIGMIGST 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 251 SERQqldfstgkvrhpgDQRQDPNIYDYCAAKTLYISDSD-KRKYFDLNAQFFYGCGMEIGGFVSQRIKVISKPSKKKQS 329
Cdd:pfam09271  77 SDQE-------------TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQS 143

                  ....*
gi 1831513092 330 MKNTD 334
Cdd:pfam09271 144 LKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
512-614 7.99e-55

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: 181.50  E-value: 7.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 512 PISPCPVVGSLEVDGHGEASRVELHGRDFKPNLKVWFGATPVETTFRSEESLHCSIPPVSQVRNEQTHwmftnrTTGDVE 591
Cdd:cd01176     1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRW------VRQPVQ 74
                          90       100
                  ....*....|....*....|...
gi 1831513092 592 VPISLVRDDGVVYSSGLTFSYKS 614
Cdd:cd01176    75 VPISLVRNDGIIYPTGLTFTYTP 97
TIG_SUH pfam20144
TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless ...
517-612 5.30e-35

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


Pssm-ID: 466305  Cd Length: 92  Bit Score: 127.33  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 517 PVVGSLEVDGHGEASRVELHGRDFKPNLKVWFGATPVETTFRSEESLHCSIPPVSQVRNEQTHWMFTNRttgdVEVPISL 596
Cdd:pfam20144   1 PVVSSLTVNGGGENAMLELHGENFTRDLKVWFGDIKAETEYRSRESLVCVVPDASELLSSWTSQKDRKK----KKVPLLL 76
                          90
                  ....*....|....*.
gi 1831513092 597 VRDDGVVYSSGLTFSY 612
Cdd:pfam20144  77 VRGDGVIYKTGLTFTY 92
 
Name Accession Description Interval E-value
BTD pfam09270
Beta-trefoil DNA-binding domain; Members of this family of DNA binding domains adopt a ...
365-490 4.46e-77

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: 240.69  E-value: 4.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 365 EGNAFHASSTKWGAFTIHLFDDERGLQEtdNFAVRDGFVYYGSVVKLVDSVTGIALPRLRIRKVDKQQVILDAscsEEPV 444
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQE--NFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDA---DEPV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831513092 445 SQLHKCAFQMIDNELVYLCLSHDKIIQHQATAI--NEHRHQINDGAAW 490
Cdd:pfam09270  76 SQLHKCAFQMKDTERMYLCLSQEKIIQFQATPCpkDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
171-334 1.02e-64

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: 209.48  E-value: 1.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 171 ISIFHAKVAQKSYGNEKRFFCPPPCIYLIGQGWKLKKdrvaQLYKTLKASAQKDAAIENDPIHEQQATELVAYIGIGSDT 250
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWKTKS----TALSPDNPLTAPRVTISISGEDSAEESQCIAWIGMIGST 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 251 SERQqldfstgkvrhpgDQRQDPNIYDYCAAKTLYISDSD-KRKYFDLNAQFFYGCGMEIGGFVSQRIKVISKPSKKKQS 329
Cdd:pfam09271  77 SDQE-------------TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQS 143

                  ....*
gi 1831513092 330 MKNTD 334
Cdd:pfam09271 144 LKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
512-614 7.99e-55

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: 181.50  E-value: 7.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 512 PISPCPVVGSLEVDGHGEASRVELHGRDFKPNLKVWFGATPVETTFRSEESLHCSIPPVSQVRNEQTHwmftnrTTGDVE 591
Cdd:cd01176     1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRW------VRQPVQ 74
                          90       100
                  ....*....|....*....|...
gi 1831513092 592 VPISLVRDDGVVYSSGLTFSYKS 614
Cdd:cd01176    75 VPISLVRNDGIIYPTGLTFTYTP 97
TIG_SUH pfam20144
TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless ...
517-612 5.30e-35

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


Pssm-ID: 466305  Cd Length: 92  Bit Score: 127.33  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 517 PVVGSLEVDGHGEASRVELHGRDFKPNLKVWFGATPVETTFRSEESLHCSIPPVSQVRNEQTHWMFTNRttgdVEVPISL 596
Cdd:pfam20144   1 PVVSSLTVNGGGENAMLELHGENFTRDLKVWFGDIKAETEYRSRESLVCVVPDASELLSSWTSQKDRKK----KKVPLLL 76
                          90
                  ....*....|....*.
gi 1831513092 597 VRDDGVVYSSGLTFSY 612
Cdd:pfam20144  77 VRGDGVIYKTGLTFTY 92
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
515-613 7.09e-21

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: 87.72  E-value: 7.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 515 PCPVVGSLEVDG-HGEASRVELHGRDfKPNLKVWFGAT-------PVETTFRSEE-SLHCSIPPVSQVRNEQThwmftnr 585
Cdd:cd00602     2 PICRVSSLSGSVnGGDEVFLLCDKVN-KPDIKVWFGEKgpgetvwEAEAMFRQEDvRQVAIVFKTPPYHNKWI------- 73
                          90       100
                  ....*....|....*....|....*...
gi 1831513092 586 tTGDVEVPISLVRDDGVVYSSGLTFSYK 613
Cdd:cd00602    74 -TRPVQVPIQLVRPDDRKRSEPLTFTYT 100
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
513-614 1.03e-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: 47.07  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513092 513 ISP--CPVVGSLEVDGHGEasrvelhGRDFKPNLKVWFGA-TPVETTFRSEESLHCSIPPVsqvrneqthwmftnRTTGD 589
Cdd:cd00102     6 ISPssGPVSGGTEVTITGS-------NFGSGSNLRVTFGGgVPCSVLSVSSTAIVCTTPPY--------------ANPGP 64
                          90       100
                  ....*....|....*....|....*
gi 1831513092 590 VEVPISLVRDDGVVYSSGLTFSYKS 614
Cdd:cd00102    65 GPVEVTVDRGNGGITSSPLTFTYVP 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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