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 351059932  142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRYGEYAIDEETVDGIL 221
Cdd:pfam00651   5 REQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVDDLL 84

                          90       100
                  ....*....|....*....|...
gi 351059932  222 HLAHLYDMPFPIKRCEEFLVDSS 244
Cdd:pfam00651  85 AAADKLQIPSLVDKCEEFLIKSL 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 351059932  142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRYGEYAIDEETVDGIL 221
Cdd:pfam00651   5 REQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVDDLL 84

                          90       100
                  ....*....|....*....|...
gi 351059932  222 HLAHLYDMPFPIKRCEEFLVDSS 244
Cdd:pfam00651  85 AAADKLQIPSLVDKCEEFLIKSL 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 351059932   149 DVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGILHLAHLY 227
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYtGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 351059932   228 DMPFPIKRCEEFLVDSS 244
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 351059932  10 LSHVFKDVSKLE-DGNTFYGPEEEHFNVQWRIVLIHQKED-----VAVFLRYLHPKNEQAPWKIDSEFTLKLSN-SSGKS 82
Cdd:cd00121    1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIYPNGDGesgdyLSLYLELDKGESDLEKWSVRAEFTLKLVNqNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 351059932  83 VTKTGSDIWNSYD--ALGFCDVFEWDSLLKDY-LIDDVIIIEVAVK 125
Cdd:cd00121   81 LSKSFTHVFFSEKgsGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126

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 351059932  142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRYGEYAIDEETVDGIL 221
Cdd:pfam00651   5 REQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVDDLL 84

                          90       100
                  ....*....|....*....|...
gi 351059932  222 HLAHLYDMPFPIKRCEEFLVDSS 244
Cdd:pfam00651  85 AAADKLQIPSLVDKCEEFLIKSL 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 351059932   149 DVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGILHLAHLY 227
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYtGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 351059932   228 DMPFPIKRCEEFLVDSS 244
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 351059932  10 LSHVFKDVSKLE-DGNTFYGPEEEHFNVQWRIVLIHQKED-----VAVFLRYLHPKNEQAPWKIDSEFTLKLSN-SSGKS 82
Cdd:cd00121    1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIYPNGDGesgdyLSLYLELDKGESDLEKWSVRAEFTLKLVNqNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 351059932  83 VTKTGSDIWNSYD--ALGFCDVFEWDSLLKDY-LIDDVIIIEVAVK 125
Cdd:cd00121   81 LSKSFTHVFFSEKgsGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. 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 351059932 144 NEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRYGEYA----IDEETVDG 219
Cdd:cd18287   19 NEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKALLKYIYTGRLtltdLKEDVLLD 98

                         90
                 ....*....|.
gi 351059932 220 ILHLAHLYDMP 230
Cdd:cd18287   99 VLGLAHQYGFE 109

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins; This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They 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. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. 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 351059932 147 FSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGILHLAH 225
Cdd:cd18186    1 LCDVTLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDVSPEAFEALLDYIYtGELELSEENVEELLAAAD 80

                 ..
gi 351059932 226 LY 227
Cdd:cd18186   81 KL 82

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also called Kelch-like protein 27 (KLHL27) or actin-binding protein IPP, is an actin-binding protein that may play a role in organizing the actin cytoskeleton. 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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18256   15 RGQHEFCDVQLQVGMELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPDIFHILLDFIYtGVVEVTVSNVQEL 94

                         90       100
                 ....*....|....*....|
gi 351059932 221 LHLAHLYDMPFPIKRCEEFL 240
Cdd:cd18256   95 LVAADMLQLTEVVEICCEFL 114

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 30 (KLHL30); KLHL30 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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18259   27 RSNPKLSDVTLLVGGREFPCHRSVLALCSHYFNAMFTGDFVESISARVEIKDVDPAVMESLIDFAYtGKLTINQGNVEAL 106

                         90       100
                 ....*....|....*....|
gi 351059932 221 LHLAHLYDMPFPIKRCEEFL 240
Cdd:cd18259  107 IRTSNRLQFPTVRKVCSRYL 126

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a component of a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 causes autosomal-dominant retinitis pigmentosa. 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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18237   16 RKQKTLCDVILIVEGREIKAHRVVLAAASHFFHLMFTSNMTESKSSEVELKDAEPDIIELLVEFAYtARISVNSNNVQSL 95

                         90       100
                 ....*....|....*....|
gi 351059932 221 LHLAHLYDMPFPIKRCEEFL 240
Cdd:cd18237   96 LDAANQYQIEPVKKMCVDFL 115

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 20 (KLHL20); KLHL20, also called Kelch-like ECT2-interacting protein (KLEIP) or Kelch-like protein X, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. KLHL20 plays a role in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells. It also controls endothelial migration and sprouting angiogenesis. 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 351059932 133 PKKKLKSFE--RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRYGEY 210
Cdd:cd18249    7 PRQTLEAINllRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVTIRDIDERAMELLIDFAYTSQ 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 351059932 211 AIDEET-VDGILHLAHLYDMPFPIKRCEEFL 240
Cdd:cd18249   87 ITVEEGnVQTLLPAACLLQLAEIQEVCCEFL 117

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL2 and KLHL3; The family includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 and KLHL3 each functions as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins. They contain a BTB domain and kelch repeat domains, 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 351059932 138 KSFE-----RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYA 211
Cdd:cd18235    7 KAFDvmnelRKQNLLCDVILVADGVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDGKALLLLIDYVYtAEIQ 86

                         90       100       110
                 ....*....|....*....|....*....|
gi 351059932 212 IDEETVDGILHLAHLYDMPFPIKRCEEFLV 241
Cdd:cd18235   87 VTEENVQVLLPAANLLQLTDVRDACCDFLQ 116

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 21 (KLHL21); KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 also targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively. 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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18250   16 RAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMFAGELRESRADRVVLHGVSAEILGLLLDFSYtGRVTVTQDNVEAL 95

                         90       100
                 ....*....|....*....|
gi 351059932 221 LHLAHLYDMPFPIKRCEEFL 240
Cdd:cd18250   96 LRAADLFQFPSVKEACCAYL 115

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 351059932 144 NEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRYGEyAIDEETVDGILHL 223
Cdd:cd18286   14 NGEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVSFVLLFIYGG-VLDLPDDVNLGEL 92

                 ....*.
gi 351059932 224 AHLYDM 229
Cdd:cd18286   93 LSLADM 98

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 1 (KLHL1); KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. It may play a role in organizing the actin cytoskeleton the brain cells. KLHL1 contains a BTB domain and kelch repeat domains, 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 351059932 135 KKLKSFERsNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAID 213
Cdd:cd18335    8 RKMESYLK-QQQLCDVILIAGNRKIPAHRLVLSAVSDYFAAMFTSDVCEAKQEEIKMEGIDPNALWDLVQFAYtGCLELK 86

                         90       100
                 ....*....|....*....|....*...
gi 351059932 214 EETVDGILHLAHLYDMPFPIKRCEEFLV 241
Cdd:cd18335   87 EDTIENLLAAACLLQLSQVVEVCCHFLM 114

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 351059932 144 NEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLL-GNFAEADKSEVKLQ--DINSTDFQNLMEVRY-GEYAIDEETVDG 219
Cdd:cd18292   14 NEELSDIVLRVGGKVFHAHRLILAKSSDVFRVMLSnDWWSESKQSEIELVedPECAAVFEKFLRYLYtGQISVNLETALP 93

                         90       100
                 ....*....|....*....|
gi 351059932 220 ILHLAHLYDMPFPIKRCEEF 239
Cdd:cd18292   94 LLMLADKYNVTDLKQLCVDF 113

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the second BTB 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 351059932 147 FSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADK-----SEVKLQDINSTDFQNLMEVRYGEYA-IDEETVDGI 220
Cdd:cd18296   17 FPDVCFQVEGHRFPCHKAFFCGRSDYFKALLRDHFAESEEnngsiPVVTLHDVSPEVFAIVLYYIYTDDTdLPPENAYDV 96

                         90
                 ....*....|
gi 351059932 221 LHLAHLYDMP 230
Cdd:cd18296   97 LYVADMYLLP 106

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4); KBTBD4, also called BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates. 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 351059932 144 NEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLME-VRYGEYAIDEETVDGILH 222
Cdd:cd18272   29 DGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARNRVIELKDVSESVFQLLVDyIYHGTVKLRVEELQETYE 108

                         90
                 ....*....|....*....
gi 351059932 223 LAHLYDMPFPIKRCEEFLV 241
Cdd:cd18272  109 VADMYQLTALFEECSRFLA 127

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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18253   13 RDSRLFTDVIICVEGREFPCHRAILSACSSYFRAMFCNDHRESREMLVEINGILAEAMDCFLQYVYtGKVKITTENVQYL 92

                         90       100
                 ....*....|....*....|
gi 351059932 221 LHLAHLYDMPFPIKRCEEFL 240
Cdd:cd18253   93 FETSSLFQISPLRDACAKFL 112

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6; This family includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. 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 351059932 144 NEEFSDVILAVGDKKFFVL----RKFLASHSTYFETLLLGNFAEaDKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVD 218
Cdd:cd18282    4 NELMADVHFIVGPPGGTQRipahKYVLATGSSVFYAMFYGGLAE-NKNEIEIPDVEPAAFLNLLRYLYcDEIDLEPDTVL 82

                         90       100
                 ....*....|....*....|....*
gi 351059932 219 GILHLAHLYDMPFPIKRCEEFLVDS 243
Cdd:cd18282   83 ATLYAAKKYLVPHLARACVQFLETS 107

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 4 (KLHL4); KLHL4 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It may be associated with X-linked cleft palate (CPX) and is also a candidate gene in the impairment of mullerian duct development. In addition, it has been identified as a target of insulin-like growth factor binding protein 5 (IGFBP5). KLHL4 contains a BTB domain and kelch repeat domains, 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 351059932 144 NEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGILH 222
Cdd:cd18336   16 HKQLCDVLLIAGNLKIPAHRLVLSAVSDYFAAMFTNDVREAKQEEIKMEGVDPDALKALVHYAYtGVLELKEDTIESLLA 95

                         90
                 ....*....|....*....
gi 351059932 223 LAHLYDMPFPIKRCEEFLV 241
Cdd:cd18336   96 AACLLQLSQVIDVCCNFLM 114

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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18240   12 RLEGKLCDVVIRVNGVEFPAHRNILCACSPYFRALFTNGWNETEKKVYKIPGVSPEMMELIIEYAYtRTVPITAENVEEL 91

                         90       100
                 ....*....|....*....|..
gi 351059932 221 LHLAHLYDMPFPIKRCEEFLVD 242
Cdd:cd18240   92 LPAADQFNIMGIVKACCDFLED 113

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL40 and KLHL41; This family includes Kelch-like proteins, KLHL40 and KLHL41. KLHL40 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. KLHL41 is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. They both contain 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 351059932 147 FSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGILHLAH 225
Cdd:cd18269   27 FVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYtSEIDLNDQNVQDIFALAS 106

                         90
                 ....*....|....*
gi 351059932 226 LYDMPFPIKRCEEFL 240
Cdd:cd18269  107 RFQIPSIFTVCVSYL 121

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 12 (KBTBD12); KBTBD12, also called Kelch domain-containing protein 6 (KLHDC6), 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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18276   16 KELAELTDVVLVAEGEKFPCHRLVLAAFSPYFKAMFTCGLMECSQREVVLHDITAESVSIILNYMYsSDLHLTNSNVQGV 95

                         90       100
                 ....*....|....*....|....*..
gi 351059932 221 LHLAHLYDMPFPIKRCEEFLVDSSEKS 247
Cdd:cd18276   96 ATAAFFLQMEDIFSVCQKYMMDHMDAS 122

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. 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 351059932 142 RSNEEFSDVILAVGDKKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQDINSTDFQNLMEVRY-GEYAIDEETVDGI 220
Cdd:cd18306   13 RKNRQFCDVILQVGGHEIPAHRAVLACASPYLFELFSSDSDGESILTVKLDGLDPDAVEVLVNYAYtSRLEVPADLVKSV 92

                         90       100
                 ....*....|....*....|..
gi 351059932 221 LHLAHLYDMPFPIKRCEEFLVD 242
Cdd:cd18306   93 YSAAKKLKMDRVKKACGDFLLE 114

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins; GCL proteins are nuclear envelope proteins highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in embryos. Both, human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 2 (GMCL2), also called germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L), may function in spermatogenesis. They may also be substrate-specific adaptors of E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. They contain BTB and BACK domains. 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 351059932 144 NEEFSDV-ILAVGdkKFFVLRKFLASHSTYFETLLLGNFAEADKSEVKLQ--DINSTdfQNLMEVRYG-----EYAIDEE 215
Cdd:cd18305   12 NGENSDItICALG--REWKLHKIYLCQSGYFASMFSGSWKESKETVINLEipDDNIT--VEALNVVFGslyrdEIEIKPS 87

                         90       100
                 ....*....|....*....|....*...
gi 351059932 216 TVDGILHLAHLYDMPFPIKRCEEFLVDS 243
Cdd:cd18305   88 RVVSILAAATLLQLDGLIQQCSEVMKET 115

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 6 (BTBD6); BTBD6, also termed lens BTB domain protein, is a BTB-domain-containing Kelch-like protein required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. 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 351059932 143 SNEEFSDVILAVG----DKKFFVLRKFLASHSTYFETLLLGNFAEaDKSEVKLQDINSTDFQNLMEVRYG-EYAIDEETV 217
Cdd:cd18349    4 NNELMADVHFIVGppgaSQRVPAHKYVLAVGSSVFYAMFYGDLAE-VKSEIHIPDVEPAAFLILLKYMYSdEIDLEADTV 82

                         90       100
                 ....*....|....*....|....*.
gi 351059932 218 DGILHLAHLYDMPFPIKRCEEFLVDS 243
Cdd:cd18349   83 LATLYAAKKYIVPALAKACVNFLETS 108