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Conserved domains on  [gi|6323137|ref|NP_013209|]
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uncharacterized protein YLR108C [Saccharomyces cerevisiae S288C]

Protein Classification

BTB/POZ domain-containing protein( domain architecture ID 13034511)

BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins; similar to Saccharomyces cerevisiae BTB/POZ domain-containing protein YLR108C

Gene Ontology:  GO:0005515
PubMed:  11340155|17120193|27521773

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 28-104 3.40e-14

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


:

Pssm-ID: 349625  Cd Length: 83  Bit Score: 67.58  E-value: 3.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137   28 FKIRIGQKLFEISGATLNSDAPNFFTQFFNTH-----DKNTILFVDRSEDVFIIIYRHLQGYFPDI-KNEVQFTCLFADA 101
Cdd:cd18316   1 VKLNVGGTLFTTSRSTLLKDPDSLLAALFSGRwplprDEDGSIFIDRDPELFRHILNFLRTGKLPLpSDFVELEELLAEA 80


                ...
gi 6323137  102 LYF 104
Cdd:cd18316  81 EFY 83
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 122-212 1.13e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.


The actual alignment was detected with superfamily member cd18316:

Pssm-ID: 453885  Cd Length: 83  Bit Score: 40.62  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137  122 NIGGVPFKVPKS-LFHEEGNRLNyfetisrisyeeieKWESNKKPGFPPLLPPSYIARSPEFFRDILSLL--GGSKLELS 198
Cdd:cd18316   4 NVGGTLFTTSRStLLKDPDSLLA--------------ALFSGRWPLPRDEDGSIFIDRDPELFRHILNFLrtGKLPLPSD 69

                        90
                ....*....|....
gi 6323137  199 EERTASLIKECRYY 212
Cdd:cd18316  70 FVELEELLAEAEFY 83
 
Name Accession Description Interval E-value
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 28-104 3.40e-14

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349625  Cd Length: 83  Bit Score: 67.58  E-value: 3.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137   28 FKIRIGQKLFEISGATLNSDAPNFFTQFFNTH-----DKNTILFVDRSEDVFIIIYRHLQGYFPDI-KNEVQFTCLFADA 101
Cdd:cd18316   1 VKLNVGGTLFTTSRSTLLKDPDSLLAALFSGRwplprDEDGSIFIDRDPELFRHILNFLRTGKLPLpSDFVELEELLAEA 80


                ...
gi 6323137  102 LYF 104
Cdd:cd18316  81 EFY 83
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 29-121 1.29e-06

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 46.53  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137      29 KIRIGQKLFEISGATLNSDAPNFFTQFFNTH---DKNTILFVDRSEDVFIIIYRHLQGYFPDIkNEVQFTCLFADALYFQ 105
Cdd:smart00225   3 TLVVGGKKFHAHKAVLAAHSPYFKALFSSDFkesDKSEIYLDDVSPEDFRALLNFLYTGKLDL-PEENVEELLELADYLQ 81

                           90
                   ....*....|....*.
gi 6323137     106 LPKLVKLIKEYDYHFT 121
Cdd:smart00225  82 IPGLVELCEEFLLKLL 97
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 122-212 1.13e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349625  Cd Length: 83  Bit Score: 40.62  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137  122 NIGGVPFKVPKS-LFHEEGNRLNyfetisrisyeeieKWESNKKPGFPPLLPPSYIARSPEFFRDILSLL--GGSKLELS 198
Cdd:cd18316   4 NVGGTLFTTSRStLLKDPDSLLA--------------ALFSGRWPLPRDEDGSIFIDRDPELFRHILNFLrtGKLPLPSD 69

                        90
                ....*....|....
gi 6323137  199 EERTASLIKECRYY 212
Cdd:cd18316  70 FVELEELLAEAEFY 83
 
Name Accession Description Interval E-value
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 28-104 3.40e-14

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349625  Cd Length: 83  Bit Score: 67.58  E-value: 3.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137   28 FKIRIGQKLFEISGATLNSDAPNFFTQFFNTH-----DKNTILFVDRSEDVFIIIYRHLQGYFPDI-KNEVQFTCLFADA 101
Cdd:cd18316   1 VKLNVGGTLFTTSRSTLLKDPDSLLAALFSGRwplprDEDGSIFIDRDPELFRHILNFLRTGKLPLpSDFVELEELLAEA 80


                ...
gi 6323137  102 LYF 104
Cdd:cd18316  81 EFY 83
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 29-121 1.29e-06

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 46.53  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137      29 KIRIGQKLFEISGATLNSDAPNFFTQFFNTH---DKNTILFVDRSEDVFIIIYRHLQGYFPDIkNEVQFTCLFADALYFQ 105
Cdd:smart00225   3 TLVVGGKKFHAHKAVLAAHSPYFKALFSSDFkesDKSEIYLDDVSPEDFRALLNFLYTGKLDL-PEENVEELLELADYLQ 81

                           90
                   ....*....|....*.
gi 6323137     106 LPKLVKLIKEYDYHFT 121
Cdd:smart00225  82 IPGLVELCEEFLLKLL 97
BTB_POZ_KCTD-like cd18316
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 122-212 1.13e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349625  Cd Length: 83  Bit Score: 40.62  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323137  122 NIGGVPFKVPKS-LFHEEGNRLNyfetisrisyeeieKWESNKKPGFPPLLPPSYIARSPEFFRDILSLL--GGSKLELS 198
Cdd:cd18316   4 NVGGTLFTTSRStLLKDPDSLLA--------------ALFSGRWPLPRDEDGSIFIDRDPELFRHILNFLrtGKLPLPSD 69

                        90
                ....*....|....
gi 6323137  199 EERTASLIKECRYY 212
Cdd:cd18316  70 FVELEELLAEAEFY 83
 
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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