NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|398365765|ref|NP_010417|]
View 

Mrx16p [Saccharomyces cerevisiae S288C]

Protein Classification

BTB/POZ domain-containing protein( domain architecture ID 13034457)

BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein similar to Arabidopsis thaliana protein ENDOPLASMIC RETICULUM-ARRESTED PEN3 that confers resistance to soil-born pathogens (e.g. the root-penetrating fungus Fusarium oxysporum) by regulating membrane trafficking, specifically mediating ABCG36/PEN3 exit from the endoplasmic reticulum and subsequent relocalization at the host-pathogen interface of the plasma membrane

Gene Ontology:  GO:0005515
PubMed:  27521773|17120193

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 30-121 1.02e-16

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: 74.90  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365765  30 KIQVGKSLFKISGASLSSDGPSFFTEYFSKkrspsnnddsnNDTMESNKNEVLFIDRSAEVFEWIYQHLQGYIIEI-KDE 108
Cdd:cd18316    2 KLNVGGTLFTTSRSTLLKDPDSLLAALFSG-----------RWPLPRDEDGSIFIDRDPELFRHILNFLRTGKLPLpSDF 70

                         90
                 ....*....|...
gi 398365765 109 VQYTMLFADAMYY 121
Cdd:cd18316   71 VELEELLAEAEFY 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 ...
 30-121 1.02e-16

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: 74.90  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365765  30 KIQVGKSLFKISGASLSSDGPSFFTEYFSKkrspsnnddsnNDTMESNKNEVLFIDRSAEVFEWIYQHLQGYIIEI-KDE 108
Cdd:cd18316    2 KLNVGGTLFTTSRSTLLKDPDSLLAALFSG-----------RWPLPRDEDGSIFIDRDPELFRHILNFLRTGKLPLpSDF 70

                         90
                 ....*....|...
gi 398365765 109 VQYTMLFADAMYY 121
Cdd:cd18316   71 VELEELLAEAEFY 83
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 30-138 8.36e-08

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: 50.00  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365765    30 KIQVGKSLFKISGASLSSDgPSFFTEYFSkkrspsnnddsnNDTMESNKNEVLFIDRSAEVFEWIYQHLQGYIIEIKDEv 109
Cdd:smart00225   3 TLVVGGKKFHAHKAVLAAH-SPYFKALFS------------SDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEE- 68

                           90       100
                   ....*....|....*....|....*....
gi 398365765   110 QYTMLFADAMYYNLPRLRSLLKETDYYFT 138
Cdd:smart00225  69 NVEELLELADYLQIPGLVELCEEFLLKLL 97
 
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 ...
 30-121 1.02e-16

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: 74.90  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365765  30 KIQVGKSLFKISGASLSSDGPSFFTEYFSKkrspsnnddsnNDTMESNKNEVLFIDRSAEVFEWIYQHLQGYIIEI-KDE 108
Cdd:cd18316    2 KLNVGGTLFTTSRSTLLKDPDSLLAALFSG-----------RWPLPRDEDGSIFIDRDPELFRHILNFLRTGKLPLpSDF 70

                         90
                 ....*....|...
gi 398365765 109 VQYTMLFADAMYY 121
Cdd:cd18316   71 VELEELLAEAEFY 83
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 30-138 8.36e-08

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: 50.00  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365765    30 KIQVGKSLFKISGASLSSDgPSFFTEYFSkkrspsnnddsnNDTMESNKNEVLFIDRSAEVFEWIYQHLQGYIIEIKDEv 109
Cdd:smart00225   3 TLVVGGKKFHAHKAVLAAH-SPYFKALFS------------SDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEE- 68

                           90       100
                   ....*....|....*....|....*....
gi 398365765   110 QYTMLFADAMYYNLPRLRSLLKETDYYFT 138
Cdd:smart00225  69 NVEELLELADYLQIPGLVELCEEFLLKLL 97
BTB_POZ_FIP2-like cd18376
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 30-136 5.28e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana FH protein interacting protein FIP2 and similar proteins; FIP2 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. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.


Pssm-ID: 349685  Cd Length: 89  Bit Score: 36.07  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365765  30 KIQVGKSLFKISGASLSSDGPSFFTEYFSKKRSpsnnddsnndtMESNKNEVLFIDRSAEVFEWIYQHLQGYIIEIKDEv 109
Cdd:cd18376    2 KLNVGGQKFTTTLDTLTKDPDSMLAAMFSGRHS-----------LKKDEDGSYFIDRDGTHFRHILNYLRDGEVKIPTE- 69

                         90       100
                 ....*....|....*....|....*..
gi 398365765 110 qytmlfadamyyNLPRLRSLLKETDYY 136
Cdd:cd18376   70 ------------DRSVLKELLEEAEYY 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH