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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152   10 FDHQMEP--YSDVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLHGEPAIFECTI 87
Cdd:pfam00651   1 LNELREQgeLCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENV 80

                          90       100
                  ....*....|....*....|....*..
gi 392889152   88 YQILLLAVKFQTYTVIKKCEKFLIHTS 114
Cdd:pfam00651  81 DDLLAAADKLQIPSLVDKCEEFLIKSL 107

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152   10 FDHQMEP--YSDVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLHGEPAIFECTI 87
Cdd:pfam00651   1 LNELREQgeLCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENV 80

                          90       100
                  ....*....|....*....|....*..
gi 392889152   88 YQILLLAVKFQTYTVIKKCEKFLIHTS 114
Cdd:pfam00651  81 DDLLAAADKLQIPSLVDKCEEFLIKSL 107

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152    19 DVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLH-GEPAIFECTIYQILLLAVKF 97
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYtGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 392889152    98 QTYTVIKKCEKFLIHTS 114
Cdd:smart00225  81 QIPGLVELCEEFLLKLL 97

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152 161 NKFTFKYT-FEKFDEDC-------VGGYNvqlgflWSLNIHRKN-----DHLRISLCCDKPEPT-PYWEVRADFQLVLPG 226
Cdd:cd00121    1 GKHTWKIVnFSELEGESiysppfeVGGYK------WRIRIYPNGdgesgDYLSLYLELDKGESDlEKWSVRAEFTLKLVN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392889152 227 QDEAPVTKGYFRNI--DEELKCEELGREIEWEEIADKY-PVDGYLTIEARV 274
Cdd:cd00121   75 QNGGKSLSKSFTHVffSEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEV 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152   10 FDHQMEP--YSDVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLHGEPAIFECTI 87
Cdd:pfam00651   1 LNELREQgeLCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENV 80

                          90       100
                  ....*....|....*....|....*..
gi 392889152   88 YQILLLAVKFQTYTVIKKCEKFLIHTS 114
Cdd:pfam00651  81 DDLLAAADKLQIPSLVDKCEEFLIKSL 107

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152    19 DVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLH-GEPAIFECTIYQILLLAVKF 97
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYtGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 392889152    98 QTYTVIKKCEKFLIHTS 114
Cdd:smart00225  81 QIPGLVELCEEFLLKLL 97

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392889152  20 VVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLHGEPAIFECTIYQILLLA 94
Cdd:cd01165    1 VVLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDASNLLELLEA 75

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152   165 FKYTFEKF-----DEDCVGGYNVQLGFLWSLNIHRKNDHLRISLCCDKPEPTP-YWEVRADFQLVLPGQDEAPVTKgYFR 238
Cdd:smart00061   2 LSHTFKNVsrleeGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSrKWSIEAEFTLKLVSQNGKSLSK-KDK 80

                           90
                   ....*....|....*
gi 392889152   239 NIDEELKCEELGREI 253
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 17 (BTBD17); BTBD17, also called galectin-3-binding protein-like, is a BTB domain-containing protein. Its function remains unclear. It may be associated with hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152  18 SDVVLVASQEWFHVSKAILCDHSPYFRCLLSNfPRIDEKPVHLLKGVNPAD----FQKFLEVL-HGEPAIFECTIYQILL 92
Cdd:cd18292   18 SDIVLRVGGKVFHAHRLILAKSSDVFRVMLSN-DWWSESKQSEIELVEDPEcaavFEKFLRYLyTGQISVNLETALPLLM 96

                         90
                 ....*....|....*..
gi 392889152  93 LAVKFQTYTVIKKCEKF 109
Cdd:cd18292   97 LADKYNVTDLKQLCVDF 113

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 15 (KLHL15); KLHL15 is a substrate-specific adaptor for the Cullin3 E3 ubiquitin-protein ligase complex that targets the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits. It also plays a key role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR), by targeting the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. KLHL15 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152  19 DVVLVASQEWFHVSKAILCDHSPYFRCLLS-NFPRIDEKPVHlLKGVNPADFQKFLEVL-HGEPAIFECTIYQILLLAVK 96
Cdd:cd18244   32 DVTLVIEDHQFQAHKALLATQSDYFRIMFTaDMRERDQDKIH-LKGLTATGFSHVLQFMyYGTIELSMLTVHEILQAAMY 110

                         90
                 ....*....|....*
gi 392889152  97 FQTYTVIKKCEKFLI 111
Cdd:cd18244  111 VQLTEVVKFCCSFLL 125

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 10 (KLHL10); KLHL10 is a substrate-specific adaptor of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins specifically in the testis during spermatogenesis. Haploinsufficiency of Klhl10 causes infertility in male mice. KLHL10 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152  19 DVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLH-GEPAIFECTIYQILLLAVKF 97
Cdd:cd18240   19 DVVIRVNGVEFPAHRNILCACSPYFRALFTNGWNETEKKVYKIPGVSPEMMELIIEYAYtRTVPITAENVEELLPAADQF 98

                         90
                 ....*....|....*
gi 392889152  98 QTYTVIKKCEKFLIH 112
Cdd:cd18240   99 NIMGIVKACCDFLED 113

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 24 (KLHL24); KLHL24, also called kainate receptor-interacting protein for GluR6 (KRIP6) or protein DRE1, is necessary to maintain the balance between intermediate filament stability and degradation, a process that is essential for skin integrity. KLHL24 is a component of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates ubiquitination of KRT14 and controls its levels during keratinocyte differentiation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152  17 YSDVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLH-GEPAIFECTIYQILLLAV 95
Cdd:cd18253   18 FTDVIICVEGREFPCHRAILSACSSYFRAMFCNDHRESREMLVEINGILAEAMDCFLQYVYtGKVKITTENVQYLFETSS 97

                         90
                 ....*....|....*
gi 392889152  96 KFQTYTVIKKCEKFL 110
Cdd:cd18253   98 LFQISPLRDACAKFL 112

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in gigaxonin; Gigaxonin, also called Kelch-like protein 16 (KLHL16), may be a cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. It may also act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, including tubulin folding cofactor B (TBCB), microtubule-associated protein MAP1B, and glial fibrillary acidic protein (GFAP). Gigaxonin is mutated in giant axonal neuropathy. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392889152  17 YSDVVLVASQEWFHVSKAILCDHSPYFRCLLS-NFPRIDEKPVHL-LKGVNPADFQKFLEVLH-GEPAIFECTIYQIL 91
Cdd:cd18245   14 LCDATLVVGGEEIPVQKNVLAAASPYFRAKLNyNPPKDDGSTYKIeLEGISVEVMEEILDYIYtGQIKLSEDNIQDIV 91

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 28 (KLHL28); KLHL28, also called BTB/POZ domain-containing protein 5 (BTBD5), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152  13 QMEPYSDVVLVASQEWFHVSKAILCDHSPYFRCLLS-NFPRIDEKPVHlLKGVNPADFQKFLEVLH-GEPAIFECTIYQI 90
Cdd:cd18257   14 QHHELCDVVLRVGDVKIHAHKVVLASCSPYFKAMFTgNLSEKENSEVE-FQCIDETALQAIVEYAYtGTVFISQATVESL 92

                         90       100
                 ....*....|....*....|
gi 392889152  91 LLLAVKFQTYTVIKKCEKFL 110
Cdd:cd18257   93 LPAANLLQIKLVLKECCDFL 112

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 7 (BTBD7); BTBD7 is a crucial regulator that is essential for region-specific epithelial cell dynamics and branching morphogenesis. It has been implicated in various cancers. BTBD7 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 392889152  18 SDVVLVASQEWFHVSKAILCDHSPYFRCLLSNFP 51
Cdd:cd18283    3 TDVDLVFQGTCFPVHRAILSARCPFFRDLLSSSP 36

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8); BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889152  18 SDVVLVASQEWFHVSKAILCDHSPYFRCLLSNFPRIDEKPVHLLKGVNPADFQKFLEVLHG----EPaiFECTIYQILLL 93
Cdd:cd18286   18 SDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVSFVLLFIYGgvldLP--DDVNLGELLSL 95

                 .
gi 392889152  94 A 94
Cdd:cd18286   96 A 96