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 17534629    12 FKNVSKLKVGKFAWTPMKEHFNVSWQIAItrthFRNEEKMEIQVGCQKLTKDDVPAGVEGEFTIKLTNSSGISTSKSSRL 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQI----YRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTH 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17534629    92 KLVKNGGLGFLK-IVWKVMQDEYLIDDSIIIEATVKI 127
Cdd:pfam00917  77 VFEKPKGWGWGKfISWDDLEKDYLVDDSITVEAHVKI 113

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 17534629    150 DVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGILHLAHMY 228
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYtGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*
gi 17534629    229 DIPLPIRKCEEFLIE 243
Cdd:smart00225  81 QIPGLVELCEEFLLK 95

MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534629    12 FKNVSKLKVGKFAWTPMKEHFNVSWQIAItrthFRNEEKMEIQVGCQKLTKDDVPAGVEGEFTIKLTNSSGISTSKSSRL 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQI----YRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTH 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17534629    92 KLVKNGGLGFLK-IVWKVMQDEYLIDDSIIIEATVKI 127
Cdd:pfam00917  77 VFEKPKGWGWGKfISWDDLEKDYLVDDSITVEAHVKI 113

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 17534629   8 LTHIFKNVSKLK-VGKFAWTPMKEHFNVSWQIAITRTHFRNEEK-MEIQVGCQKLTKDDVPAGVEGEFTIKLTNSSG--- 82
Cdd:cd00121   1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIYPNGDGESGDyLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGgks 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17534629  83 ISTSKSSRLKLVKNGGLGFLKIV-WKVMQDEY-LIDDSIIIEATVK 126
Cdd:cd00121  81 LSKSFTHVFFSEKGSGWGFPKFIsWDDLEDSYyLVDDSLTIEVEVK 126

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 17534629    150 DVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGILHLAHMY 228
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYtGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*
gi 17534629    229 DIPLPIRKCEEFLIE 243
Cdd:smart00225  81 QIPGLVELCEEFLLK 95

MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534629    12 FKNVSKLKVGKFAWTPMKEHFNVSWQIAItrthFRNEEKMEIQVGCQKLTKDDVPAGVEGEFTIKLTNSSGISTSKSSRL 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQI----YRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTH 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17534629    92 KLVKNGGLGFLK-IVWKVMQDEYLIDDSIIIEATVKI 127
Cdd:pfam00917  77 VFEKPKGWGWGKfISWDDLEKDYLVDDSITVEAHVKI 113

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 17534629 143 QSKEKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGI 221
Cdd:cd18257  13 RQHHELCDVVLRVGDVKIHAHKVVLASCSPYFKAMFTGNLSEKENSEVEFQCIDETALQAIVEYAYtGTVFISQATVESL 92

                        90       100
                ....*....|....*....|
gi 17534629 222 LHLAHMYDIPLPIRKCEEFL 241
Cdd:cd18257  93 LPAANLLQIKLVLKECCDFL 112

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 17534629 146 EKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GE---PAIDDDTVDGI 221
Cdd:cd18287  20 EEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKALLKYIYtGRltlTDLKEDVLLDV 99

                        90
                ....*....|
gi 17534629 222 LHLAHMYDIP 231
Cdd:cd18287 100 LGLAHQYGFE 109

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 8 (KLHL8); KLHL8 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for the ubiquitination and degradation of rapsyn, a postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. 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 17534629 136 KPLKCFDQ--SKEKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPA 212
Cdd:cd18238   1 DSFKVLHQfyENGELCDVTLKVGEKSIHCHRLVLACVSPYFRAMFTSEMAESKQDSITIKDIDEEAVELLVDFAYtGKLT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17534629 213 IDDDTVDGILHLAHMYDIPLPIRKCEEFlievseksMKDQL 253
Cdd:cd18238  81 LTVDNVQSLLYAASLLQVEEVAKACCEF--------MKDHL 113

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534629      8 LTHIFKNVSKLKVGKFAWTPMKEHFNVSWQIAItrthFRNEEKMEIQVGCQKLTKDDVPAGVEGEFTIKLTNSSGISTSK 87
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKI----YRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSK 77

                           90
                   ....*....|....*...
gi 17534629     88 SSRLKLVKNGGLGFLKIV 105
Cdd:smart00061  78 KDKHVFEKPSGWGFSKFI 95

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 17534629   8 LTHIFKNVSKLK-VGKFAWTPMKEHFNVSWQIAITRTHFRNEEK-MEIQVGCQKLTKDDVPAGVEGEFTIKLTNSSG--- 82
Cdd:cd00121   1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIYPNGDGESGDyLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGgks 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17534629  83 ISTSKSSRLKLVKNGGLGFLKIV-WKVMQDEY-LIDDSIIIEATVK 126
Cdd:cd00121  81 LSKSFTHVFFSEKGSGWGFPKFIsWDDLEDSYyLVDDSLTIEVEVK 126

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 17534629 147 KFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGILHLA 225
Cdd:cd18269  26 KFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYtSEIDLNDQNVQDIFALA 105

                        90
                ....*....|....*.
gi 17534629 226 HMYDIPLPIRKCEEFL 241
Cdd:cd18269 106 SRFQIPSIFTVCVSYL 121

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 17534629 143 QSKEKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGI 221
Cdd:cd18259  27 RSNPKLSDVTLLVGGREFPCHRSVLALCSHYFNAMFTGDFVESISARVEIKDVDPAVMESLIDFAYtGKLTINQGNVEAL 106

                        90       100
                ....*....|....*....|
gi 17534629 222 LHLAHMYDIPLPIRKCEEFL 241
Cdd:cd18259 107 IRTSNRLQFPTVRKVCSRYL 126

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as a substrate-specific adaptor for a Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A. 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 17534629 144 SKEKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGIL 222
Cdd:cd18247  15 RQGKLCDVTLKVGDQKFSAHRIVLAATIPYFHAMFTHDMVESKQDEITMQGIEPSALEALINFAYsGRIAIDTSNVQSLL 94

                        90       100
                ....*....|....*....|.
gi 17534629 223 HLAHMYDIPLPIRKCEEFLIE 243
Cdd:cd18247  95 VGASFLQLQSVKDACCEFLKE 115

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 2 (KBTBD2); KBTBD2, also called BTB and kelch domain-containing protein 1 (BKLHD1), plays an essential role in the regulation of insulin-signaling pathway. It is a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase, which targets p85alpha, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85alpha ubiquitination and proteasome-mediated degradation. 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 17534629 138 LKCFDQsKEKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDD 216
Cdd:cd18270  17 LKFFYE-QQLLTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAATLQIIITYAYtGNLAINDS 95

                        90       100
                ....*....|....*....|....*..
gi 17534629 217 TVDGILHLAHMYDIPLPIRKCEEFLIE 243
Cdd:cd18270  96 TVEQLYETACFLQVEDVLQRCREYLIK 122

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 17534629 146 EKFSDVILAVGDQKFFVLRKFLASHSTFFESRFL-GNFDEADKSEVTLRDID--SADFQNLLEVLY-GEPAIDDDTVDGI 221
Cdd:cd18292  15 EELSDIVLRVGGKVFHAHRLILAKSSDVFRVMLSnDWWSESKQSEIELVEDPecAAVFEKFLRYLYtGQISVNLETALPL 94

                        90
                ....*....|....*....
gi 17534629 222 LHLAHMYDIPLPIRKCEEF 240
Cdd:cd18292  95 LMLADKYNVTDLKQLCVDF 113

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 17534629 143 QSKEKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGI 221
Cdd:cd18250  16 RAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMFAGELRESRADRVVLHGVSAEILGLLLDFSYtGRVTVTQDNVEAL 95

                        90       100
                ....*....|....*....|
gi 17534629 222 LHLAHMYDIPLPIRKCEEFL 241
Cdd:cd18250  96 LRAADLFQFPSVKEACCAYL 115

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 6 (KLHL6); KLHL6 is a BTB-kelch protein with a lymphoid tissue-restricted expression pattern. It is involved in B-lymphocyte antigen receptor signaling and germinal center formation. It belongs to the KLHL gene family, which is composed of an N-terminal BTB-POZ domain and four to six Kelch motifs in tandem. 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 17534629 149 SDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLYGEPA-IDDDTVDGILHLAHM 227
Cdd:cd18236  25 TDVILCVDSQEFSCHRVVLAAASNYFRAMFCNDLKEKYEEKIIIKGVDAETMQILLDYTYTSKVlITKQNVQRVLEAASL 104

                        90
                ....*....|....*.
gi 17534629 228 YDIPLPIRKCEEFLIE 243
Cdd:cd18236 105 FQFLRMVDACASFLTE 120

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like ECH-associated protein 1 (KEAP1); KEAP1, also called cytosolic inhibitor of Nrf2 (INrf2) or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. 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 17534629 146 EKFSDVILAVG----DQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDG 220
Cdd:cd18248  19 QQLCDVTLKVKyqdpKEEFMAHKVVLASSSPYFKAMFTSGLRECGMEVVPIEGVHPCVMSRLIEFAYtASISVGEKCVLH 98

                        90       100
                ....*....|....*....|...
gi 17534629 221 ILHLAHMYDIPLPIRKCEEFLIE 243
Cdd:cd18248  99 VLPGAVMYQMDSVVKACCDFLEQ 121

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 17534629 138 LKCFDQSKEK--FSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAID 214
Cdd:cd18253   6 LQVFNEFRDSrlFTDVIICVEGREFPCHRAILSACSSYFRAMFCNDHRESREMLVEINGILAEAMDCFLQYVYtGKVKIT 85

                        90       100       110
                ....*....|....*....|....*....|
gi 17534629 215 DDTVDGILHLAHMYDIpLPIRK-CEEFLIE 243
Cdd:cd18253  86 TENVQYLFETSSLFQI-SPLRDaCAKFLEE 114

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing proteins KBTBD6 and KBTBD7; KBTBD6 and KBTBD7 are substrate adaptors of a cullin-3 RING ubiquitin ligase complex that mediates ubiquitylation and proteasomal degradation of T-lymphoma and metastasis gene 1 (TIAM1), a RAC1-specific guanine exchange factor (GEF), by cooperating with gamma-aminobutyric acid receptor-associated proteins (GABARAP). KBTBD7 may also act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling. 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 17534629 157 DQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGILHLAHMYDIPLPIR 235
Cdd:cd18273  43 GRLFPCNRNVLAAASPYFKSMFTGGLYESKQETVTIHDVDSESMALIIDYCYtGRVTLSEANVQRLYAAANMLQLEYVRE 122

                ....*.
gi 17534629 236 KCEEFL 241
Cdd:cd18273 123 ACASFL 128

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
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17534629 150 DVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY 208
Cdd:cd18249  25 DVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVTIRDIDERAMELLIDFAY 83

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 3 (KBTBD3); KBTBD3, also called BTB and kelch domain-containing protein 3 (BKLHD3), 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 17534629 148 FSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGILHLAH 226
Cdd:cd18271  24 FFDFNIIVKDETIPCHRCVLAACSDFFRAMFEVNMKERDDGSVTISNLSPKAVKAFLDYAYtGKAEITDDNVEMFFQMSS 103

                        90
                ....*....|....*..
gi 17534629 227 MYDIPLPIRKCEEFLIE 243
Cdd:cd18271 104 FLQVSLLSKACSDFLIK 120

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 17534629 146 EKFSDVILAVG----DQKFFVLRKFLASHSTFFESRFLGNFDEaDKSEVTLRDIDSADFQNLLEVLYG-EPAIDDDTVDG 220
Cdd:cd18349   6 ELMADVHFIVGppgaSQRVPAHKYVLAVGSSVFYAMFYGDLAE-VKSEIHIPDVEPAAFLILLKYMYSdEIDLEADTVLA 84

                        90       100
                ....*....|....*....|.
gi 17534629 221 ILHLAHMYDIPLPIRKCEEFL 241
Cdd:cd18349  85 TLYAAKKYIVPALAKACVNFL 105

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also called HIB homolog 2 or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes may contain homodimeric SPOPL or the heterodimers formed by speckle-type POZ protein (SPOP) and SPOPL, which are less efficient than ubiquitin ligase complexes containing only SPOP. 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 17534629 147 KFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY--GEPAIdDDTVDGILHL 224
Cdd:cd18343  20 RFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYtgKAPNL-DKMADNLLAA 98

                        90
                ....*....|....*..
gi 17534629 225 AHMYDIPLPIRKCEEFL 241
Cdd:cd18343  99 ADKYALERLKVMCEEAL 115

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL9 and KLHL13; KLHL9 and KLHL13 (also called BTB and kelch domain-containing protein 2, or BKLHD2) are substrate-specific adaptors of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes, thereby coordinating faithful mitotic progression and completion of cytokinesis. They 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 17534629 138 LKCFDQ--SKEKFSDVILAVGD--QKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPA 212
Cdd:cd18239  11 LQGFDQlrGEGLLCDVTLVPGDgdETFPVHRAMMASASDYFKAMFTGGMKEQELMCIKLHGVSKIGLKNIIDFIYtAKLS 90

                        90       100       110
                ....*....|....*....|....*....|.
gi 17534629 213 IDDDTVDGILHLAHMYDIpLPIRK-CEEFLI 242
Cdd:cd18239  91 LNMDNLQDTLEAASFLQI-LPVLDfCKVLLI 120

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 17534629 150 DVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-GEPAIDDDTVDGILHLAHMY 228
Cdd:cd18235  23 DVILVADGVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDGKALLLLIDYVYtAEIQVTEENVQVLLPAANLL 102

                        90
                ....*....|...
gi 17534629 229 DIPLPIRKCEEFL 241
Cdd:cd18235 103 QLTDVRDACCDFL 115

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in plant BTB/POZ-MATH (BPM) protein family; The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins from other plants. BPM protein, also called protein BTB-POZ and MATH domain, 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. 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 17534629 146 EKFSDVILAVGDQKFFVLRKFLASHSTFFESRFLGNFDEADKSEVTLRDIDSADFQNLLEVLY-------------GEPA 212
Cdd:cd18280  12 EEGADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVFKALLHFIYkdelpddvepagsDSSS 91

                        90       100
                ....*....|....*....|....*.
gi 17534629 213 IDDDTVDGILHLAHMYDIPLPIRKCE 238
Cdd:cd18280  92 LDTTMAQHLLAAADRYALERLRLLCE 117