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 334187759 189 LGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltlllivysr 268
Cdd:cd18280    1 LGQHFGALLESEEGADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVF-------------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187759 269 myhpgsspgalllfsslltrdKVLLHFIYWDELPDMQELIGTDSTLASTLVAQHLLAAADRYALERLKAICESKLC 344
Cdd:cd18280   67 ---------------------KALLHFIYKDELPDDVEPAGSDSSSLDTTMAQHLLAAADRYALERLRLLCESRLC 121

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 334187759  34 GFHEFKICGYSLAKGvgvgKYVASDTFMVGGYSWAIYFYPDGKSpeDNSSYVSLFIALASEGAD-----VRALFELTLVD 108
Cdd:cd00121    1 GKHTWKIVNFSELEG----ESIYSPPFEVGGYKWRIRIYPNGDG--ESGDYLSLYLELDKGESDlekwsVRAEFTLKLVN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334187759 109 QSGnGKHKVHSHFgraldsgPYTLKYRGSMWGYKRFFRRSSLESSDYLKENSLLVRCRV 167
Cdd:cd00121   75 QNG-GKSLSKSFT-------HVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125

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 334187759 189 LGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltlllivysr 268
Cdd:cd18280    1 LGQHFGALLESEEGADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVF-------------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187759 269 myhpgsspgalllfsslltrdKVLLHFIYWDELPDMQELIGTDSTLASTLVAQHLLAAADRYALERLKAICESKLC 344
Cdd:cd18280   67 ---------------------KALLHFIYKDELPDDVEPAGSDSSSLDTTMAQHLLAAADRYALERLRLLCESRLC 121

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 334187759  34 GFHEFKICGYSLAKGvgvgKYVASDTFMVGGYSWAIYFYPDGKSpeDNSSYVSLFIALASEGAD-----VRALFELTLVD 108
Cdd:cd00121    1 GKHTWKIVNFSELEG----ESIYSPPFEVGGYKWRIRIYPNGDG--ESGDYLSLYLELDKGESDlekwsVRAEFTLKLVN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334187759 109 QSGnGKHKVHSHFgraldsgPYTLKYRGSMWGYKRFFRRSSLESSDYLKENSLLVRCRV 167
Cdd:cd00121   75 QNG-GKSLSKSFT-------HVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125

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 334187759   204 DVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltlllivysrmyhpgsspgalllfs 283
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDF----------------------------- 51

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187759   284 slltrdKVLLHFIYWDELPDMQELIgtdstlastlvaQHLLAAADRYALERLKAICESKLCE 345
Cdd:smart00225  52 ------RALLNFLYTGKLDLPEENV------------EELLELADYLQIPGLVELCEEFLLK 95

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 334187759 189 LGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltlllivysr 268
Cdd:cd18280    1 LGQHFGALLESEEGADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVF-------------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187759 269 myhpgsspgalllfsslltrdKVLLHFIYWDELPDMQELIGTDSTLASTLVAQHLLAAADRYALERLKAICESKLC 344
Cdd:cd18280   67 ---------------------KALLHFIYKDELPDDVEPAGSDSSSLDTTMAQHLLAAADRYALERLRLLCESRLC 121

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 334187759  34 GFHEFKICGYSLAKGvgvgKYVASDTFMVGGYSWAIYFYPDGKSpeDNSSYVSLFIALASEGAD-----VRALFELTLVD 108
Cdd:cd00121    1 GKHTWKIVNFSELEG----ESIYSPPFEVGGYKWRIRIYPNGDG--ESGDYLSLYLELDKGESDlekwsVRAEFTLKLVN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334187759 109 QSGnGKHKVHSHFgraldsgPYTLKYRGSMWGYKRFFRRSSLESSDYLKENSLLVRCRV 167
Cdd:cd00121   75 QNG-GKSLSKSFT-------HVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 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 334187759  193 LGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltlllivysrmyhp 272
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDF------------------ 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187759  273 gsspgalllfsslltrdKVLLHFIYWDELPDMQELigtdstlastlvaQHLLAAADRYALERLKAICESKLCE 345
Cdd:pfam00651  63 -----------------EALLEFMYTGKLISEENV-------------DDLLAAADKLQIPSLVDKCEEFLIK 105

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP) and similar proteins; This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill and similar proteins. Both, SPOP and SPOPL, serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domains. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. 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 334187759 185 PVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltllli 264
Cdd:cd18279    1 PECRLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVF---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187759 265 vysrmyhpgsspgalllfsslltrdKVLLHFIYWDELPDMQELigtdstlastlvAQHLLAAADRYALERLKAICESKLC 344
Cdd:cd18279   71 -------------------------KEMMRFIYTGKAPNLDKM------------ADDLLAAADKYALERLKVMCEDALC 113

                 ....*..
gi 334187759 345 EGVAINT 351
Cdd:cd18279  114 SNLSVEN 120

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in TD and POZ domain-containing proteins (TDPOZ); TDPOZ is a family of bipartite animal and plant proteins that contains a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. This subfamily contains only mammalian members. Plant TDPOZ proteins contain a MATH domain at the N-terminal region and are named "BTB/POZ and MATH domain-containing proteins (BPM)", not included in this subfamily. 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 334187759 182 IPVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltl 261
Cdd:cd18344    3 IKDPRHMLTDDLGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEERLKNPIEIHDLDPQVF------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187759 262 llivysrmyhpgsspgalllfsslltrdKVLLHFIYWDELPdmqeligtdsTLASTLVAQHLLAAADRYALERLKAICES 341
Cdd:cd18344   76 ----------------------------KEMMGFIYTGKAP----------HLHSHSMACDVLAAADKYGLEGLKVLCED 117

                        170
                 ....*....|
gi 334187759 342 KLCEGVAINT 351
Cdd:cd18344  118 ALCRNLSVEN 127

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; This family includes ABTB2, BTBD11, plant ARM repeat protein interacting with ABF2 (ARIA), and similar proteins. ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2. 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 334187759 204 DVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFkvlpltlllivysrmyhpgsspgalllfs 283
Cdd:cd18297   14 DVTFLVEGRPFYAHKIVLVTASDRFKSMLSSGSTEAQTPVIEIPDIRYDIF----------------------------- 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187759 284 slltrdKVLLHFIYWDelpdmqeliGTDSTLASTLVAQHLLAAADRYALERLKAICESkLCEG 346
Cdd:cd18297   65 ------QLMMQYLYTG---------GVESLDVAQDDALELLRAASFFQLDGLKRHCEI-LLSQ 111

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 334187759 187 SNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEdmeapifkvlpltlllivy 266
Cdd:cd18286    2 SRLGKDLLQLFLNGEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLT------------------- 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187759 267 srmyhpGSSPGALLlfsslltrdkVLLHFIYWD--ELPDMQELIgtdstlastlvaqHLLAAADRYALERLKAICESKL 343
Cdd:cd18286   63 ------GVSHAAVS----------FVLLFIYGGvlDLPDDVNLG-------------ELLSLADMYGLDGLKDVVAYTL 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187759 186 VSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVL 257
Cdd:cd18287    6 VHFLSEDIGALFLNEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKAL 77

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing 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 334187759 189 LGQQLGNLLESGKGCDVVFQV--DGETFNAHKLVLATRSPVFNAQLF-GPLGDRNTKCITIEDMEAPIFkvlpltllliv 265
Cdd:cd18294    1 FAADMKSLINNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRAMFLtGPQKESTQSPLVLSDIEPEVF----------- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187759 266 ysrmyhpgsspgalllfsslltrdKVLLHFIYwdelpdmqeligTDSTLASTLVAQHLLAAADRYALERLKAICE 340
Cdd:cd18294   70 ------------------------RAVLEFIY------------TNCVTLSNHTVIEVLAAAVEYGLDELRKLCE 108

first 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 first 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 334187759 188 NLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNT-KCITIEDMEAPIFKvlplTLLLIVY 266
Cdd:cd18285    1 HLSQDLLRLLREELHTDVTFYVGSTLFKAHKAILLARVPEFFSHIIGKLSSLEDqEPINIENLEASEFK----TFLRQVY 76

                 .
gi 334187759 267 S 267
Cdd:cd18285   77 T 77

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE 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 334187759 186 VSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSpvfnaQLFGPLGDRNTKCITIEDmeapifkvlpltlllIV 265
Cdd:cd18303    2 ISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARS-----EKWSNENLASTNELDLSD---------------IS 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187759 266 YSRMYhpgsspgalllfsslltrdkVLLHFIYWDELPDMQEligtDSTLAStlvaqhLLAAADRYALERLKAICESKL 343
Cdd:cd18303   62 YEVVL--------------------ALLRWLYTDELDLTLD----DEFLLE------LMKAAKRFQLTDLVERCERAL 109

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187759 191 QQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVL 257
Cdd:cd18247    8 PVMEEIRRQGKLCDVTLKVGDQKFSAHRIVLAATIPYFHAMFTHDMVESKQDEITMQGIEPSALEAL 74

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187759    38 FKICGYSLAKGVGVGKYVASDTFMVGGYSWAIYFYPDGKspednssYVSLFIALASEGAD-----VRALFELTLVDQSGN 112
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNG-------FLSLYLHCEKEECDsrkwsIEAEFTLKLVSQNGK 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 334187759   113 G-KHKVHSHFGraldsgpytlkyRGSMWGYKRFF 145
Cdd:smart00061  74 SlSKKDKHVFE------------KPSGWGFSKFI 95

Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to human SPOP. SPOP was isolated as a novel antigen recognized by serum from a scleroderma patient, whose overexpression in COS cells results in a discrete speckled pattern in the nuclei. It contains an N-terminal MATH domain and a C-terminal BTB (also called POZ) domain. Together with Cul3, SPOP constitutes an ubiquitin E3 ligase which is able to ubiquitinate the PcG protein BMI1, the variant histone macroH2A1 and the death domain-associated protein Daxx. Therefore, SPOP may be involved in the regulation of these proteins and may play a role in transcriptional regulation, apoptosis and X-chromosome inactivation. Cul3 binds to the BTB domain of SPOP whereas Daxx and the macroH2A1 nonhistone region have been shown to bind to the MATH domain. Both MATH and BTB domains are necessary for the nuclear speckled accumulation of SPOP. There are many proteins, mostly uncharacterized, containing both MATH and BTB domains from C. elegans and plants which are excluded from this family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187759  40 ICGYSLAKGvGVGKYVASDTFMVGG---YSWAIYFYPDGKSpEDNSSYVSLFIALAS-EGADVRALFELTLVDQSGNGKH 115
Cdd:cd03774   11 ISNFSFCRE-EMGEVIKSSTFSSGAndkLKWCLRVNPKGLD-EESKDYLSLYLLLVScPKSEVRAKFKFSILNAKGEETK 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187759 116 KVHSH-FGRALdsgpytlkyRGSMWGYKRFFRRSSL--ESSDYLKENSLLVRCRVGVV 170
Cdd:cd03774   89 AMESQrAYRFV---------QGKDWGFKKFIRRDFLldEANGLLPDDKLTLFCEVSVV 137

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Dictyostelium discoideum trishanku and similar proteins; Trishanku is a novel regulator required for normal morphogenesis and cell-type stability in Dictyostelium discoideum. It contains a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187759 197 LESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIF 254
Cdd:cd18314    1 YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIF 58

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
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187759 191 QQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIED 248
Cdd:cd18238    4 KVLHQFYENGELCDVTLKVGEKSIHCHRLVLACVSPYFRAMFTSEMAESKQDSITIKD 61

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187759 191 QQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVL 257
Cdd:cd18257    7 QGLNLLRQHHELCDVVLRVGDVKIHAHKVVLASCSPYFKAMFTGNLSEKENSEVEFQCIDETALQAI 73

BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal to a BTB domain, in a diverse set of architectures together with Kelch, MATH, and/or TAZ domains. It is involved in interactions with the Cullin3 (Cul3) ubiquitin ligase complex, as well as in homo-oligomerization. Most proteins containing the BACK domain are understood to function as adaptor proteins that play a role in ubiquitination of various substrates.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187759 349 INTVATTLALAEQHHCLQLKAVCLKFVAlpENLKAVMQTDGFDYLkesCPSLLTELLQ 406
Cdd:cd14733    2 PENCLGILELADLYNLEELKEKALKFIL--ENFEEVSKSEEFLEL---SVELLLELLS 54

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
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187759 204 DVVFQVDG----ETFNAHKLVLATRSPVFNAQLFGPLGDrNTKCITIEDMEAPIFKVL 257
Cdd:cd18282    9 DVHFIVGPpggtQRIPAHKYVLATGSSVFYAMFYGGLAE-NKNEIEIPDVEPAAFLNL 65

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 9 (ZBTB9); ZBTB9 may be involved in transcriptional regulation. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187759 200 GKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFgpLGDrnTKCITIED-MEAPIFKvlplTLLLIVYS 267
Cdd:cd18200   16 GKFCDLSVHVQGRVFRAHKAVLAASSPYFHDKLL--LND--TNCLVLPSvIEAAAFE----NLLQLIYS 76

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 37 (ZBTB37); ZBTB37 may be involved in transcriptional regulation. It is differentially expressed in aryl hydrocarbon receptor (AhR)-KO mice compared with WT mice, and may potentially contribute to the aging phenotype of AhR-KO mice. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187759 181 NIPVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLfgPLGDRNTKCITI 246
Cdd:cd18222    4 EIPDFSNSVLSHLNQLRMQGRLCDIVVNVQGQSFRAHKVVLAASSPYFRDHM--SLNEMSTVSISV 67

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 34 (ZBTB34); ZBTB34 acts as a transcriptional regulator. It downregulates specificity protein (Sp) transcription factors Sp1, Sp3, and Sp4 in pancreatic cancer cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 334187759 180 YNIPVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVF 228
Cdd:cd18220    3 FDVPEYSNTVLSQLNELRLQGKLCDIIVHIQGQPFRAHKAVLAASSPYF 51

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 43 (ZBTB43); ZBTB43, also called zinc finger and BTB domain-containing protein 22B (ZBTB22b), zinc finger protein 297B (ZNF297B), or ZnF-x, may be involved in transcriptional regulation. It interacts with BDP1, a subunit of transcription factor IIIB (TFIIIB). Since BDP1 is essential in Pol III transcription, ZBTB43 may also regulate these transcriptional pathways. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187759 187 SNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFgplgDRNTKCITIEDMEAPifKVLPLTLLLIVY 266
Cdd:cd18227   10 STILQKLNQQRQQGQLCDISVVVQGHLFRAHKAVLAASSPYFCDQVL----LKNSRRIVLPDVMNP--RVFENILLSCYT 83

                         90       100
                 ....*....|....*....|
gi 334187759 267 SRMYHPGSSPGALLLFSSLL 286
Cdd:cd18227   84 GRLVLPAPEIVSYLTAASFL 103

BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein (SPOP) and similar proteins; This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill, and similar proteins. Both SPOP and SPOPL serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also termed Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334187759 349 INTVATTLALAEQHHCLQLKAVCLKFVALpeNLKAVMQTDGFDYLKESCPSLLTE 403
Cdd:cd14821    3 VENAAEVLVLADLHSAEQLKTHAIDFINS--HATDVMETEGWKSMVRSHPHLVAE 55

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 22 (ZBTB22); ZBTB22, also called protein BING1 or zinc finger protein 297, may be involved in transcriptional regulation. Its gene, together with BING 3-5, TAPASIN, DAXX, RGL2, and HKE2, form a dense cluster at the centromeric end of the major histocompatibility complex class I region. ZBTB22 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 334187759 183 PVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQL 232
Cdd:cd18210    2 PEITSSLLESLNQQRMEGKLCDISIHVQGRVFRAHRAVLAASSPYFHDQV 51

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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334187759 203 CDVVFQVDGETFNAHKLVLATRSPVFNAQL--FGPLGDRNTKCITIEDMEAPIFK 255
Cdd:cd18245   15 CDATLVVGGEEIPVQKNVLAAASPYFRAKLnyNPPKDDGSTYKIELEGISVEVME 69

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187759 197 LESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVL 257
Cdd:cd18272   27 LEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARNRVIELKDVSESVFQLL 87

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
                 ....*....|....*....|....*....|....*....|....*...
gi 334187759 203 CDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDME 250
Cdd:cd18249   24 CDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVTIRDID 71

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2; This family includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187759 203 CDVVFQVDGETFN----AHKLVLATRSPVFNAQLFGPLGDRNTKcITIEDMEAPIFkvlpLTLLLIVYS 267
Cdd:cd18281   23 SDVHFIVGKGDNEqripAHKFVLSIGSAVFDAMFNGGMATTSAE-IELPDVEPAAF----LALLRFLYS 86