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Conserved domains on  [gi|1572047571|ref|NP_501189|]
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BTB domain-containing protein [Caenorhabditis elegans]

Protein Classification

BTB/POZ domain-containing protein( domain architecture ID 10459331)

BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein similar to Arabidopsis thaliana BTB/POZ domain-containing proteins

Gene Ontology:  GO:0005515
PubMed:  27521773|17120193

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 130-231 8.09e-13

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


:

Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 64.20  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047571 130 FIDFEKKNSWLDALIRSEDgkKMMYANSGILALNSPILKQKLQNDKKAH----IIIPSESFAAMEKLMNFLHPPYKMERE 205
Cdd:pfam00651   1 LNELREQGELCDVTLVVGD--KEFRAHKAVLAACSPYFKALFSGQESESsvseITLDDVSPEDFEALLEFMYTGKLISEE 78

                          90       100
                  ....*....|....*....|....*.
gi 1572047571 206 IVEEVLDLASKWKMESVLTKYEQLLI 231
Cdd:pfam00651  79 NVDDLLAAADKLQIPSLVDKCEEFLI 104
 
Name Accession Description Interval E-value
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 130-231 8.09e-13

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 64.20  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047571 130 FIDFEKKNSWLDALIRSEDgkKMMYANSGILALNSPILKQKLQNDKKAH----IIIPSESFAAMEKLMNFLHPPYKMERE 205
Cdd:pfam00651   1 LNELREQGELCDVTLVVGD--KEFRAHKAVLAACSPYFKALFSGQESESsvseITLDDVSPEDFEALLEFMYTGKLISEE 78

                          90       100
                  ....*....|....*....|....*.
gi 1572047571 206 IVEEVLDLASKWKMESVLTKYEQLLI 231
Cdd:pfam00651  79 NVDDLLAAADKLQIPSLVDKCEEFLI 104
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 149-232 1.92e-07

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: 48.46  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047571  149 GKKMMYANSGILALNSPILKQKLQN----DKKAHIIIPSESFAAMEKLMNFLHPPY-KMEREIVEEVLDLASKWKMESVL 223
Cdd:smart00225   7 GGKKFHAHKAVLAAHSPYFKALFSSdfkeSDKSEIYLDDVSPEDFRALLNFLYTGKlDLPEENVEELLELADYLQIPGLV 86


                   ....*....
gi 1572047571  224 TKYEQLLIR 232
Cdd:smart00225  87 ELCEEFLLK 95
 
Name Accession Description Interval E-value
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 130-231 8.09e-13

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 64.20  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047571 130 FIDFEKKNSWLDALIRSEDgkKMMYANSGILALNSPILKQKLQNDKKAH----IIIPSESFAAMEKLMNFLHPPYKMERE 205
Cdd:pfam00651   1 LNELREQGELCDVTLVVGD--KEFRAHKAVLAACSPYFKALFSGQESESsvseITLDDVSPEDFEALLEFMYTGKLISEE 78

                          90       100
                  ....*....|....*....|....*.
gi 1572047571 206 IVEEVLDLASKWKMESVLTKYEQLLI 231
Cdd:pfam00651  79 NVDDLLAAADKLQIPSLVDKCEEFLI 104
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
 149-232 1.92e-07

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: 48.46  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047571  149 GKKMMYANSGILALNSPILKQKLQN----DKKAHIIIPSESFAAMEKLMNFLHPPY-KMEREIVEEVLDLASKWKMESVL 223
Cdd:smart00225   7 GGKKFHAHKAVLAAHSPYFKALFSSdfkeSDKSEIYLDDVSPEDFRALLNFLYTGKlDLPEENVEELLELADYLQIPGLV 86


                   ....*....
gi 1572047571  224 TKYEQLLIR 232
Cdd:smart00225  87 ELCEEFLLK 95
 
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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