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Conserved domains on  [gi|1046877938|ref|XP_017457355|]
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BTB/POZ domain-containing protein KCTD20 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
1-73 1.01e-52

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 cd18386:

Pssm-ID: 453885  Cd Length: 104  Bit Score: 167.06  E-value: 1.01e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIRCQD 73
Cdd:cd18386    32 MFGPGREYNFTRPNEKGEYEIAEGISCTVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIKCQD 104
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
135-174 7.98e-03

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13176:

Pssm-ID: 473070 [Multi-domain]  Cd Length: 117  Bit Score: 35.33  E-value: 7.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1046877938 135 GEEYSQILYS--SKLYRFfkyieNRDVAKtvLKERGLKNIRI 174
Cdd:cd13176     2 GEEDEEVLFShrAKLYRF-----DKDVKQ--WKERGVGDIKI 36
 
Name Accession Description Interval E-value
BTB_POZ_KCTD20 cd18386
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-73 1.01e-52

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20); KCTD20, also called potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349694  Cd Length: 104  Bit Score: 167.06  E-value: 1.01e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIRCQD 73
Cdd:cd18386    32 MFGPGREYNFTRPNEKGEYEIAEGISCTVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIKCQD 104
BTB_3 pfam16017
BTB/POZ domain;
1-78 6.02e-46

BTB/POZ domain;


Pssm-ID: 464976  Cd Length: 106  Bit Score: 149.79  E-value: 6.02e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIRCQDLSALL 78
Cdd:pfam16017  29 MFGSSMERNFTRPNEKGEYEIAEGISSTVFRAILDYYKTGVIRCPPSVSIPELREACDYLLIPFDATTIKCQNLRALL 106
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
135-174 7.98e-03

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 35.33  E-value: 7.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1046877938 135 GEEYSQILYS--SKLYRFfkyieNRDVAKtvLKERGLKNIRI 174
Cdd:cd13176     2 GEEDEEVLFShrAKLYRF-----DKDVKQ--WKERGVGDIKI 36
 
Name Accession Description Interval E-value
BTB_POZ_KCTD20 cd18386
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-73 1.01e-52

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20); KCTD20, also called potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349694  Cd Length: 104  Bit Score: 167.06  E-value: 1.01e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIRCQD 73
Cdd:cd18386    32 MFGPGREYNFTRPNEKGEYEIAEGISCTVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIKCQD 104
BTB_3 pfam16017
BTB/POZ domain;
1-78 6.02e-46

BTB/POZ domain;


Pssm-ID: 464976  Cd Length: 106  Bit Score: 149.79  E-value: 6.02e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIRCQDLSALL 78
Cdd:pfam16017  29 MFGSSMERNFTRPNEKGEYEIAEGISSTVFRAILDYYKTGVIRCPPSVSIPELREACDYLLIPFDATTIKCQNLRALL 106
BTB_POZ_BTBD10_GMRP1 cd18385
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-79 3.53e-45

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 10 (BTBD10); BTBD10, also called glucose metabolism-related protein 1 (GMRP1), plays a major role as an activator of AKT family members. It binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. It also plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells. BTBD10 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.


Pssm-ID: 349693  Cd Length: 110  Bit Score: 147.91  E-value: 3.53e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCINFDFNTIRCQDLSALLH 79
Cdd:cd18385    32 MFGSGREHNFTRPNEKGEYEVAEGISSTVFRAILDYYKTGIIRCPDGISIPELREACDYLCISFDYSTIKCRDLSALMH 110
BTB_POZ_KCTD20-like cd18318
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-63 2.05e-39

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20) and BTB/POZ domain-containing protein 10 (BTBD10); KCTD20, also termed potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. BTBD10, also termed glucose metabolism-related protein 1 (GMRP1), plays a major role as an activator of AKT family members. It binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. It also plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells.


Pssm-ID: 349627  Cd Length: 92  Bit Score: 132.44  E-value: 2.05e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046877938   1 MFGPGREYNFTRPNEKGEYEIAEGISATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYLCIN 63
Cdd:cd18318    30 MFGSGLENNFTRPNERGEYEVADGISATVFRAILDYYKTGIIRCPPSVSVAELREACDYLLIP 92
BTB_POZ_Kv_KCTD cd18187
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-60 1.49e-19

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins; This family includes two protein groups: voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins. Kv channels are membrane proteins with fundamental physiological roles. They are responsible for a variety of electrical phenomena, such as the repolarization of the action potential, spike frequency adaptation, synaptic repolarization, and smooth muscle contraction. 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. All family members contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.


Pssm-ID: 349498  Cd Length: 83  Bit Score: 80.60  E-value: 1.49e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046877938   1 MFGPGREynFTRPNEKGEYEIAEgiSATVFRTVLDYYKTGIINCPDGISIPDLRDTCDYL 60
Cdd:cd18187    28 MFKPGRE--FTFPNETGEYFIDR--DPTVFRTILNYYRTGKLNCPDGISIPDLREECDFY 83
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
135-174 7.98e-03

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 35.33  E-value: 7.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1046877938 135 GEEYSQILYS--SKLYRFfkyieNRDVAKtvLKERGLKNIRI 174
Cdd:cd13176     2 GEEDEEVLFShrAKLYRF-----DKDVKQ--WKERGVGDIKI 36
 
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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