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Conserved domains on  [gi|1751363296|ref|NP_001361332|]
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recombining binding protein suppressor of hairless isoform 4 [Homo sapiens]

Protein Classification

BTD and IPT_RBP-Jkappa domain-containing protein( domain architecture ID 10558084)

protein containing domains LAG1-DNAbind, BTD, and IPT_RBP-Jkappa

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 ...
 192-314 1.31e-88

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: 266.50  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 192 EGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHK 271
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQENFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDADEPVSQLHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1751363296 272 CAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMINDGASW 314
Cdd:pfam09270  81 CAFQMKDTERMYLCLSQEKIIQFQATPCPKDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
 34-164 1.40e-70

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: 221.03  E-value: 1.40e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296  34 VLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWK--------------KKKEQMERDGCSEQESQPCAFIGI--GNSDQE 97
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWKtkstalspdnpltaPRVTISISGEDSAEESQCIAWIGMigSTSDQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751363296  98 MQQLNLEGKNYCTAKTLYISDSD-KRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNAD 164
Cdd:pfam09271  81 TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQSLKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
 336-432 2.38e-69

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: 216.17  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 336 PVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLV 415
Cdd:cd01176     1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVRQPVQVPISLV 80

                          90
                  ....*....|....*..
gi 1751363296 416 RNDGIIYSTSLTFTYTP 432
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 ...
 192-314 1.31e-88

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: 266.50  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 192 EGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHK 271
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQENFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDADEPVSQLHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1751363296 272 CAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMINDGASW 314
Cdd:pfam09270  81 CAFQMKDTERMYLCLSQEKIIQFQATPCPKDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
 34-164 1.40e-70

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: 221.03  E-value: 1.40e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296  34 VLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWK--------------KKKEQMERDGCSEQESQPCAFIGI--GNSDQE 97
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWKtkstalspdnpltaPRVTISISGEDSAEESQCIAWIGMigSTSDQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751363296  98 MQQLNLEGKNYCTAKTLYISDSD-KRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNAD 164
Cdd:pfam09271  81 TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQSLKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
 336-432 2.38e-69

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: 216.17  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 336 PVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLV 415
Cdd:cd01176     1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVRQPVQVPISLV 80

                          90
                  ....*....|....*..
gi 1751363296 416 RNDGIIYSTSLTFTYTP 432
Cdd:cd01176    81 RNDGIIYPTGLTFTYTP 97
TIG_SUH pfam20144
TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless ...
 341-430 1.85e-46

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


Pssm-ID: 466305  Cd Length: 92  Bit Score: 156.22  E-value: 1.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 341 PVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRW--VRQPVQVPVTLVRND 418
Cdd:pfam20144   1 PVVSSLTVNGGGENAMLELHGENFTRDLKVWFGDIKAETEYRSRESLVCVVPDASELLSSWTSqkDRKKKKVPLLLVRGD 80

                          90
                  ....*....|..
gi 1751363296 419 GIIYSTSLTFTY 430
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 ...
 192-314 1.31e-88

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: 266.50  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 192 EGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHK 271
Cdd:pfam09270   1 EGGAFHASSTQWGAFTIHLLDDNQGEQENFTVRDGFICYGSVVKLVCSVTGVALPPLIIRKVDKQQVILDADEPVSQLHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1751363296 272 CAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMINDGASW 314
Cdd:pfam09270  81 CAFQMKDTERMYLCLSQEKIIQFQATPCPKDPNREVLNDGACW 123
LAG1-DNAbind pfam09271
LAG1, DNA binding; Members of this family are found in various eukaryotic hypothetical ...
 34-164 1.40e-70

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: 221.03  E-value: 1.40e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296  34 VLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWK--------------KKKEQMERDGCSEQESQPCAFIGI--GNSDQE 97
Cdd:pfam09271   1 VIILHAKVAQKSYGTEKRFLCPPPCVYLLGPGWKtkstalspdnpltaPRVTISISGEDSAEESQCIAWIGMigSTSDQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751363296  98 MQQLNLEGKNYCTAKTLYISDSD-KRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNAD 164
Cdd:pfam09271  81 TQQLDLVVWGRCAAKTLYISDSDeKRKHFELLVKLFAPNGQEIGSFESKPIKVISKPSKKRQSLKNAD 148
IPT_RBP-Jkappa cd01176
IPT domain of the recombination signal Jkappa binding protein (RBP-Jkappa). RBP-J kappa, was ...
 336-432 2.38e-69

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: 216.17  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 336 PVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLV 415
Cdd:cd01176     1 PVTPVPVVSSLELNGGGDVAMLELHGENFTPNLKVWFGDVEAETMYRCEESLLCVVPDISAFREEWRWVRQPVQVPISLV 80

                          90
                  ....*....|....*..
gi 1751363296 416 RNDGIIYSTSLTFTYTP 432
Cdd:cd01176    81 RNDGIIYPTGLTFTYTP 97
TIG_SUH pfam20144
TIG domain; This entry represents a TIG-like domain found in the suppressor of hairless ...
 341-430 1.85e-46

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


Pssm-ID: 466305  Cd Length: 92  Bit Score: 156.22  E-value: 1.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 341 PVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRW--VRQPVQVPVTLVRND 418
Cdd:pfam20144   1 PVVSSLTVNGGGENAMLELHGENFTRDLKVWFGDIKAETEYRSRESLVCVVPDASELLSSWTSqkDRKKKKVPLLLVRGD 80

                          90
                  ....*....|..
gi 1751363296 419 GIIYSTSLTFTY 430
Cdd:pfam20144  81 GVIYKTGLTFTY 92
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 338-432 1.66e-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: 113.92  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 338 TPVPVVESLQLNG-GGDVAMLELTGQNFtPNLRVWFGD-------VEAETMYRCGE-SMLCVVPDISAFREGWrwVRQPV 408
Cdd:cd00602     1 LPICRVSSLSGSVnGGDEVFLLCDKVNK-PDIKVWFGEkgpgetvWEAEAMFRQEDvRQVAIVFKTPPYHNKW--ITRPV 77

                          90       100
                  ....*....|....*....|....
gi 1751363296 409 QVPVTLVRNDGIIYSTSLTFTYTP 432
Cdd:cd00602    78 QVPIQLVRPDDRKRSEPLTFTYTP 101
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 341-432 1.34e-10

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


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 57.86  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 341 PVVESLQLN----GGGDVAMLELTGQNFTPNLRVWF-GDVEAETMYRCGESMLCVVPdisAFREGWrwvrqPVQVPVTLV 415
Cdd:cd00102     1 PVITSISPSsgpvSGGTEVTITGSNFGSGSNLRVTFgGGVPCSVLSVSSTAIVCTTP---PYANPG-----PGPVEVTVD 72

                          90
                  ....*....|....*..
gi 1751363296 416 RNDGIIYSTSLTFTYTP 432
Cdd:cd00102    73 RGNGGITSSPLTFTYVP 89
IPT_PCSR cd00603
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
 341-432 1.15e-03

IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.


Pssm-ID: 238337 [Multi-domain]  Cd Length: 90  Bit Score: 38.20  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 341 PVVESLQ-----LNGGgdvAMLELTGQNFT---PNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGwrwvrqPVQVPV 412
Cdd:cd00603     1 PVITSISpssgpLSGG---TRLTITGSNLGsgsPRVRVTVGGVPCKVLNVSSTEIVCRTPAAATPGEG------PVEVTV 71

                          90       100
                  ....*....|....*....|
gi 1751363296 413 TlVRNDGIIYSTSLTFTYTP 432
Cdd:cd00603    72 D-GANVSARVLSNTTFTYVE 90
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 340-432 1.47e-03

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: 38.23  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751363296 340 VPVVE-----SLQLNGGGDVAmleLTGQNFTPNLRVWFGD----------VEAET-MYRCGESML-CVVPDISAFRegwr 402
Cdd:cd01178     1 LPEIEkkslnSCSVNGGEELF---LTGKNFLKDSKVVFQEkgqdgeaqweAEATIdKEKSHQNHLvVEVPPYHNKH---- 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1751363296 403 wVRQPVQVPVTLVRNDGiIYSTSLTFTYTP 432
Cdd:cd01178    74 -VAAPVQVQFYVVNGKR-KRSQPQTFTYTP 101
 
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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