BACK (BTB and C-terminal Kelch) 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. BPM protein, also termed 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332640837 308 CEGISINTVATTLALAEQHHCFQLKAACLKFIAlpENLKAVMETDGFDYLKESCPSLLSELLEY 371
Cdd:cd14736    1 CEGVDVNTVATTLALAEQHHASQLKAVCLKFVA--RNLAAVMQTDGFEYLKESCPSLQSELLKT 62

BACK (BTB and C-terminal Kelch) 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. BPM protein, also termed 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332640837 308 CEGISINTVATTLALAEQHHCFQLKAACLKFIAlpENLKAVMETDGFDYLKESCPSLLSELLEY 371
Cdd:cd14736    1 CEGVDVNTVATTLALAEQHHASQLKAVCLKFVA--RNLAAVMQTDGFEYLKESCPSLQSELLKT 62

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 332640837  33 GSHEFKISGYSLvkgmGIGKYVASDTFMVGGYSWAIYFYPDGKSPEDNsvYVSLFIALASEGAD-----VRALFELTLVD 107
Cdd:cd00121    1 GKHTWKIVNFSE----LEGESIYSPPFEVGGYKWRIRIYPNGDGESGD--YLSLYLELDKGESDlekwsVRAEFTLKLVN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332640837 108 QSGNERHKVHSHFGRTlesgpytlKYRGSMWGYKRFFKRSLLESSDYLKDNGLLVRCCV 166
Cdd:cd00121   75 QNGGKSLSKSFTHVFF--------SEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332640837    37 FKISGYSLVKGMGIGKYVASDTFMVGGYSWAIYFYPDGKspednsvYVSLFIALASEGAD-----VRALFELTLVDQSGN 111
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNG-------FLSLYLHCEKEECDsrkwsIEAEFTLKLVSQNGK 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 332640837   112 ER-HKVHSHFGrtlesgpytlkyRGSMWGYKRFF 144
Cdd:smart00061  74 SLsKKDKHVFE------------KPSGWGFSKFI 95

BACK (BTB and C-terminal Kelch) 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. BPM protein, also termed 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332640837 308 CEGISINTVATTLALAEQHHCFQLKAACLKFIAlpENLKAVMETDGFDYLKESCPSLLSELLEY 371
Cdd:cd14736    1 CEGVDVNTVATTLALAEQHHASQLKAVCLKFVA--RNLAAVMQTDGFEYLKESCPSLQSELLKT 62

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 332640837  33 GSHEFKISGYSLvkgmGIGKYVASDTFMVGGYSWAIYFYPDGKSPEDNsvYVSLFIALASEGAD-----VRALFELTLVD 107
Cdd:cd00121    1 GKHTWKIVNFSE----LEGESIYSPPFEVGGYKWRIRIYPNGDGESGD--YLSLYLELDKGESDlekwsVRAEFTLKLVN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332640837 108 QSGNERHKVHSHFGRTlesgpytlKYRGSMWGYKRFFKRSLLESSDYLKDNGLLVRCCV 166
Cdd:cd00121   75 QNGGKSLSKSFTHVFF--------SEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins; 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 332640837 184 PVSGLGQQFGKLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWD 263
Cdd:cd18345    1 PECRLSDDLGLLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVMREMLRFIYTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332640837 264 EMPDMQDLigtdlkwastlvAQHLLAAADRYALERLRTICESKLCEGISINTV 316
Cdd:cd18345   81 KAPNLDKM------------ADDLLAAADKYALERLKVMCEEALCSNLSVENV 121

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 332640837 184 PVSGLGQQFGKLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWD 263
Cdd:cd18279    1 PECRLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332640837 264 EMPDMQDLigtdlkwastlvAQHLLAAADRYALERLRTICESKLCEGISINT 315
Cdd:cd18279   81 KAPNLDKM------------ADDLLAAADKYALERLKVMCEDALCSNLSVEN 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 332640837 181 IPVPVSGLGQQFGKLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFI 260
Cdd:cd18344    3 IKDPRHMLTDDLGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEERLKNPIEIHDLDPQVFKEMMGFI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332640837 261 YWDEMPDMQdligtdlkwaSTLVAQHLLAAADRYALERLRTICESKLCEGISINT 315
Cdd:cd18344   83 YTGKAPHLH----------SHSMACDVLAAADKYGLEGLKVLCEDALCRNLSVEN 127

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP); SPOP, also called HIB homolog 1 or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins, such as BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. 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 332640837 181 IPVPVSGLGQQFGKLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFI 260
Cdd:cd18342    2 VKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332640837 261 YWDEMPDMQDLigtdlkwastlvAQHLLAAADRYALERLRTICESKLCEGISI 313
Cdd:cd18342   82 YTGKAPNLDKM------------ADDLLAAADKYALERLKVMCEDALCSNLSV 122

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. 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 332640837 194 KLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMPDMQDLIG 273
Cdd:cd18300    2 LFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGNFRESSAKEVELPGVSKETFLALLEYLYTDQAPILEDGDC 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332640837 274 TDlkwastlvaqhLLAAADRYALERLRTICESKL 307
Cdd:cd18300   82 VG-----------LIVLANRLCLPRLVALCEQYI 104

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 332640837 188 LGQQFGKLLESGKGADVTFEV--DGETFPAHKLVLAARSAVFRAQLFGPLRSENTNC-IIIEDVQAPIFKMLLHFIYWDE 264
Cdd:cd18294    1 FAADMKSLINNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRAMFLTGPQKESTQSpLVLSDIEPEVFRAVLEFIYTNC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 332640837 265 MPDMQDLigtdlkwastlvAQHLLAAADRYALERLRTICE 304
Cdd:cd18294   81 VTLSNHT------------VIEVLAAAVEYGLDELRKLCE 108

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 332640837 191 QFGKLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMPdmqd 270
Cdd:cd18256   10 QLNKLRGQHEFCDVQLQVGMELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPDIFHILLDFIYTGVVE---- 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 332640837 271 lIGTDlkwastlVAQHLLAAADRYALERLRTICESKLCE 309
Cdd:cd18256   86 -VTVS-------NVQELLVAADMLQLTEVVEICCEFLKG 116

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 332640837 202 ADVTFEVDG----ETFPAHKLVLAARSAVFRAQLFGPLrSENTNCIIIEDVQAPIFKMLLHFIYWDEMpdmqdligtdlk 277
Cdd:cd18282    8 ADVHFIVGPpggtQRIPAHKYVLATGSSVFYAMFYGGL-AENKNEIEIPDVEPAAFLNLLRYLYCDEI------------ 74

                         90       100
                 ....*....|....*....|....*....
gi 332640837 278 wasTLVAQHLLA---AADRYALERLRTIC 303
Cdd:cd18282   75 ---DLEPDTVLAtlyAAKKYLVPHLARAC 100

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332640837 196 LESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIY-WDEMPDMQDLIGt 274
Cdd:cd18314    1 YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYtGQVTLSEENVLD- 79

                         90       100
                 ....*....|....*....|....*....
gi 332640837 275 dlkwastlvaqhLLAAADRYALERLRTIC 303
Cdd:cd18314   80 ------------LLMLASKYQVPDLEKLC 96

first 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 first 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 332640837 194 KLLESGKGADVTFEVDGETFPAHKLVLAARSAVFrAQLFGPlRSENTNCIIIED--VQAPIFKMLLHFIYWD----EMPD 267
Cdd:cd18295   12 RLLEQGSYSDVTFNVHGESFPAHRCILSARSPYF-AEMFET-KWKDKREINLKHplVNPDAFRALLQYLYTGrleiHVDD 89

                 ....*
gi 332640837 268 MQDLI 272
Cdd:cd18295   90 VEDCK 94

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster proteins bric-a-brac 1 (BAB1), bric-a-brac 2 (BAB2), modifier of mdg4 (doom), and similar proteins; BAB1 and BAB2 probably act as transcriptional regulators that are required for specification of the tarsal segment and are involved in antenna development. Doom is a product of the Drosophila mod(mdg4) gene. It induces apoptosis and binds to baculovirus inhibitor-of-apoptosis proteins. This subfamily also includes Drosophila melanogaster sex determination protein fruitless (FRU), protein jim lovell (LOV), zinc finger protein chinmo, transcription factor GAGA, transcription factor Ken, and longitudinals lacking proteins (LOLA). FRU probably acts as a transcriptional regulator that plays a role in male courtship behavior and sexual orientation, and enhances male-specific expression of takeout in brain-associated fat body. LOV, also called tyrosine kinase-related (TKR), has a regulatory role during midline cell development. Chinmo is a functional effector of the JAK/STAT pathway that regulates eye development, tumor formation, and stem cell self-renewal in Drosophila. GAGA is a transcriptional activator that functions by regulating chromatin structure. Ken, also termed protein Ken and Barbie, is a transcription factor required for Terminalia development. LOLA proteins are putative transcription factors required for axon growth and guidance in the central and peripheral nervous systems. Proteins in this subfamily contain a 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332640837 202 ADVTFEVDGETFPAHKLVLAARSAVFRAqLFGPLRSENTNCIIIEDVQAPIFKMLLHFIY-------WDEMPDMQDLI 272
Cdd:cd18315    2 VDVTLACEGGSLKAHKLVLAAASPYFAA-LLKETPPDEHPVIILPDVPYSELKALLDFIYtgevnvsQEQLESLLKLA 78

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332640837 188 LGQQFGKLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTN-CIIIEDVQAPIFKMLLHFIY 261
Cdd:cd18285    2 LSQDLLRLLREELHTDVTFYVGSTLFKAHKAILLARVPEFFSHIIGKLSSLEDQePINIENLEASEFKTFLRQVY 76

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 332640837 195 LLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMpdmqdligt 274
Cdd:cd18269   21 LLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEI--------- 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 332640837 275 DLKWASTlvaQHLLAAADRYALERLRTICESKL 307
Cdd:cd18269   92 DLNDQNV---QDIFALASRFQIPSIFTVCVSYL 121

Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332640837  54 VASDTFMVGGYSWAIYFYPDGKSPEDNSvYVSLFIALAS-EGADVRALFELTLVDQSGNERHKVhshfgRTLESgPYTLk 132
Cdd:cd03773   24 VYSDPLNVDGLCWRLKVYPDGNGEVRGN-FLSVFLELCSgLGEASKYEYRVEMVHQANPTKNIK-----REFAS-DFEV- 95

                         90       100
                 ....*....|....*....|....*.
gi 332640837 133 yrGSMWGYKRFFKRSLLESSDYLKDN 158
Cdd:cd03773   96 --GECWGYNRFFRLDLLINEGYLLPE 119

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 332640837 196 LESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIY 261
Cdd:cd18272   27 LEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARNRVIELKDVSESVFQLLVDYIY 92

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 26 (KLHL26); KLHL26 is encoded by the klhl26 gene, which is regulated by p53 via fuzzy tandem repeats. 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 332640837 203 DVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMP-DMQDLigtdlkwast 281
Cdd:cd18255   20 DVTLIADGQRFQAHKVVLASCSDYFRAMFTGGMRESSQDEIELKGVSAKGLKHILDFAYTSELTlDLDCI---------- 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332640837 282 lvaQHLLAAADRYALERLRTICESKLCEGISINT 315
Cdd:cd18255   90 ---QDVLGAAVHLQMLPVVELCEEFLKSAMSVEN 120

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 11 (BTBD11); BTBD11, also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11, is a BTB-domain-containing protein. 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. 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 332640837 195 LLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTnCIIIEDVQAPIFKMLLHFIYWDempdmqdliGT 274
Cdd:cd18351   18 FLNNKEMSDVTFLVEGRPFYAHKVLLFTASPRFKALLSNKPSAENT-CIEISYVKYHIFQLVMQYLYCG---------GT 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 332640837 275 DLKWASTLVAQHLLAAADRYALERLRTICESkLCEGiSINT 315
Cdd:cd18351   88 ESLLIKNNEIMELLSAAKFFQLEALQRHCEI-ICAK-SINT 126

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. 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 332640837 202 ADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMPDmqdligtdlkwAST 281
Cdd:cd18360   11 ADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCP-----------ASI 79

                         90       100
                 ....*....|....*....|....*..
gi 332640837 282 LVAQHLLAAADRYALERLRTICESKLC 308
Cdd:cd18360   80 LQAMALLICAEMYQVSRLQHICELYII 106

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 35 (KLHL35); KLHL35 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Significant differences in DNA methylation of the KLHL35 gene in abdominal aortic aneurysm (AAA) patients compared to non-AAA controls suggest a potential role in AAA pathology. Hypermethylation of the KLHL35 gene has also been associated with the development of 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 332640837 198 SGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMPDMQDligtdlk 277
Cdd:cd18265   20 SGTFTDVVLLVDGKDFPCHRATLSANSAYFRAMFGGHLKESRQAVVEIQKVSAAAMEVLLDYMYGGGLRIQED------- 92

                         90       100
                 ....*....|....*....|....*.
gi 332640837 278 wastlVAQHLLAAADRYALERLRTIC 303
Cdd:cd18265   93 -----NVESVLEASDLLQVSKLREAC 113

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 332640837 202 ADVTFEV----DGETFPAHKLVLAARSAVFRAQLFGPLrSENTNCIIIEDVQAPIFKMLLHFIYWDEMpdmqdligtDLK 277
Cdd:cd18349    9 ADVHFIVgppgASQRVPAHKYVLAVGSSVFYAMFYGDL-AEVKSEIHIPDVEPAAFLILLKYMYSDEI---------DLE 78

                         90       100
                 ....*....|....*....|....*.
gi 332640837 278 wASTLVAQhlLAAADRYALERLRTIC 303
Cdd:cd18349   79 -ADTVLAT--LYAAKKYIVPALAKAC 101

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332640837 204 VTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIY 261
Cdd:cd01165    1 VVLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLRDISPEDFRALLEFLY 58

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 41 (KLHL41); KLHL41 is also called Kel-like protein 23, Kelch repeat and BTB domain-containing protein 10 (KBTBD10), Kelch-related protein 1 (Krp1), or sarcosine. It is a novel kelch-related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. 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 332640837 194 KLLESGKGADVTFEVDGETFPAHKLVLAARSAVFRAQLFGPLRSENTNCIIIEDVQAPIFKMLLHFIYWDEMpdmqDLIG 273
Cdd:cd18341   20 ELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEESEEKKKEVVLDNVDPNIMDMILKYLYSAEI----DLND 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 332640837 274 TDLkwastlvaQHLLAAADRYALERLRTICESKLCEGISIN 314
Cdd:cd18341   96 GNV--------QDIFALASRFQIPSVFTVCVTYLQKRLSPA 128