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 18405153  25 GSHQFTIQGYSLAKGmspgKFIQSDIFSVGGYDWAIYFYPDGKNpeDQSSYISLFIALASDSND-----IRALFELTLMD 99
Cdd:cd00121   1 GKHTWKIVNFSELEG----ESIYSPPFEVGGYKWRIRIYPNGDG--ESGDYLSLYLELDKGESDlekwsVRAEFTLKLVN 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18405153 100 QSGkGKHKVHSHFdraleggPYTLKYKGSMWGYKRFFKRSALETSDYLKDDCLVINCTV 158
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 18405153   184 LKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNvhei 263
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLIS---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18405153   264 tgstsassfTNMIQHLLAAADLYDLARLKILCEVLLCEKL 303
Cdd:pfam00651  77 ---------EENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107

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 18405153 300 CEKLDVDNVATTLALAEQHQFLQLKAFCLEFVAspANLGAVMKSEGFKHLKQSCPTLLSELLNT 363
Cdd:cd14736   1 CEGVDVNTVATTLALAEQHHASQLKAVCLKFVA--RNLAAVMQTDGFEYLKESCPSLQSELLKT 62

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405153     29 FTIQGYSLAKGMSPGKFIQSDIFSVGGYDWAIYFYPDGKnpedqssYISLFIALASDSND-----IRALFELTLMDQSGK 103
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNG-------FLSLYLHCEKEECDsrkwsIEAEFTLKLVSQNGK 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 18405153    104 G-KHKVHSHFDraleggpytlkyKGSMWGYKRFF 136
Cdd:smart00061  74 SlSKKDKHVFE------------KPSGWGFSKFI 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 18405153    48 SDIFSVGGYDWAIYFYPDGKNpedqssyISLFIALASDSND-----IRALFELTLMDQSGKGKHKVHSH-FDraleggpy 121
Cdd:pfam00917  15 SPVEERFNIPWRLQIYRKGGF-------LGLYLHCDKEEELergwsIETEFTLKLVSSNGKSVTKTDTHvFE-------- 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18405153   122 tlKYKGsmWGYKRFFKRSALETsDYLKDDCLVINCTV 158
Cdd:pfam00917  80 --KPKG--WGWGKFISWDDLEK-DYLVDDSITVEAHV 111

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 18405153   184 LKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNvhei 263
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLIS---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18405153   264 tgstsassfTNMIQHLLAAADLYDLARLKILCEVLLCEKL 303
Cdd:pfam00651  77 ---------EENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107

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 18405153 175 LPLSNMGQGLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYT 254
Cdd:cd18343   3 VPECRLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYT 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18405153 255 DVLPNVHEitgstsassftnMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18343  83 GKAPNLDK------------MADNLLAAADKYALERLKVMCEEALCNNLSVEN 123

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 18405153 176 PLSNMGQGLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTD 255
Cdd:cd18279   1 PECRLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18405153 256 VLPNVHEitgstsassftnMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18279  81 KAPNLDK------------MADDLLAAADKYALERLKVMCEDALCSNLSVEN 120

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins; This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405153 194 CDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLpnvhEITgstsassfT 273
Cdd:cd18186   2 CDVTLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGEL----ELS--------E 69

                        90
                ....*....|...
gi 18405153 274 NMIQHLLAAADLY 286
Cdd:cd18186  70 ENVEELLAAADKL 82

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 18405153 184 LKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNVHEi 263
Cdd:cd18344  14 LGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEERLKNPIEIHDLDPQVFKEMMGFIYTGKAPHLHS- 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18405153 264 tgstsassfTNMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18344  93 ---------HSMACDVLAAADKYGLEGLKVLCEDALCRNLSVEN 127

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 18405153    195 DIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNVHEitgstsassftn 274
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEE------------ 68

                           90       100
                   ....*....|....*....|....*....
gi 18405153    275 MIQHLLAAADLYDLARLKILCEVLLCEKL 303
Cdd:smart00225  69 NVEELLELADYLQIPGLVELCEEFLLKLL 97

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 18405153 195 DIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYtdvlpnvheiTGST-SASSFT 273
Cdd:cd18297  14 DVTFLVEGRPFYAHKIVLVTASDRFKSMLSSGSTEAQTPVIEIPDIRYDIFQLMMQYLY----------TGGVeSLDVAQ 83

                        90       100       110
                ....*....|....*....|....*....|....
gi 18405153 274 NMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18297  84 DDALELLRAASFFQLDGLKRHCEILLSQQIDLDN 117

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains 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 18405153 180 MGQGLKDLLDSEVGCD----IAFQVGDETYKAHKLILAARSPVFRAQF----FGPIGNNNVDRIVIDDIEPSIFKAMLSF 251
Cdd:cd18301   1 FQEDFKKLLDEADEGDnihdVVFQVGGKTFPAHKFILASRSDYFRKLFlsslLTSEDAVGCDVVHIEKVPPEIFEQLLQF 80

                ....
gi 18405153 252 IYTD 255
Cdd:cd18301  81 IYTD 84

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 18405153 185 KDLLDSEVGCDIAFQVGDETYKAHKLILAARSpvfraQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNVHEIt 264
Cdd:cd18303  10 ASLFDKELYSDITIKLADKSIPAHKFVLAARS-----EKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLTLDD- 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18405153 265 gstsassftNMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18303  84 ---------EFLLELMKAAKRFQLTDLVERCERALMSSVNVDN 117

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405153 182 QGLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQF--FGPIGNNNVDRIVIDDIEPSIFKAMLSFIYtdvlpn 259
Cdd:cd18245   3 RALNSFREEPHLCDATLVVGGEEIPVQKNVLAAASPYFRAKLnyNPPKDDGSTYKIELEGISVEVMEEILDYIY------ 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18405153 260 vheiTGSTSASSFTnmIQHLLAAADLYDLARLKILCevllCEKLD 304
Cdd:cd18245  77 ----TGQIKLSEDN--IQDIVQAADLLLMTDLKDLC----CEFLE 111

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 18405153 183 GLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLpnvhE 262
Cdd:cd18269  17 GLKDLLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEI----D 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18405153 263 ITGSTsassftnmIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18269  93 LNDQN--------VQDIFALASRFQIPSIFTVCVSYLQKRLSLSN 129

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant ARM repeat protein interacting with ABF2 (ARIA) and similar proteins; 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, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. ARIA is a novel abscisic acid signaling component. It negatively regulates seed germination and young seedling growth. 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 18405153 195 DIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLpnvhEITgstsassfTN 274
Cdd:cd18352  15 DVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMRFIYTGSV----DIT--------ND 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 18405153 275 MIQHLLAAADLYDLARLKILCEVLLCEKLDVDNV 308
Cdd:cd18352  83 IAKDLLRAADQYLLEGLKRLCEYTIAQDLTLENI 116

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 18405153 183 GLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYtdvlpnvhe 262
Cdd:cd18341  17 GLKELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEESEEKKKEVVLDNVDPNIMDMILKYLY--------- 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18405153 263 itgSTSASSFTNMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18341  88 ---SAEIDLNDGNVQDIFALASRFQIPSVFTVCVTYLQKRLSPAN 129

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18405153 187 LLDSEVGCDIAFQVGD----ETYKAHKLILAARSPVFRAQFFGPIGNNNVDrIVIDDIEPSIFKAMLSFIYTD 255
Cdd:cd18282   1 MFNNELMADVHFIVGPpggtQRIPAHKYVLATGSSVFYAMFYGGLAENKNE-IEIPDVEPAAFLNLLRYLYCD 72

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 18405153 185 KDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPnvheit 264
Cdd:cd18300   1 KLFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGNFRESSAKEVELPGVSKETFLALLEYLYTDQAP------ 74

                        90       100       110
                ....*....|....*....|....*....|..
gi 18405153 265 gstSASSFTNMiqHLLAAADLYDLARLKILCE 296
Cdd:cd18300  75 ---ILEDGDCV--GLIVLANRLCLPRLVALCE 101

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 18405153 182 QGLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYtdvlpnvh 261
Cdd:cd18257   7 QGLNLLRQHHELCDVVLRVGDVKIHAHKVVLASCSPYFKAMFTGNLSEKENSEVEFQCIDETALQAIVEYAY-------- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18405153 262 eiTGSTSASSFTnmIQHLLAAADLYDLARLKILCEVLLCEKLDV 305
Cdd:cd18257  79 --TGTVFISQAT--VESLLPAANLLQIKLVLKECCDFLESQLDP 118

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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18405153 187 LLDSEVGCDIAFQVGDETYK----AHKLILAARSPVFRAQFFGPIGNNNVDrIVIDDIEPSIFKAMLSFIYTD 255
Cdd:cd18281  16 LFNNETLSDVHFIVGKGDNEqripAHKFVLSIGSAVFDAMFNGGMATTSAE-IELPDVEPAAFLALLRFLYSD 87

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405153     29 FTIQGYSLAKGMSPGKFIQSDIFSVGGYDWAIYFYPDGKnpedqssYISLFIALASDSND-----IRALFELTLMDQSGK 103
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNG-------FLSLYLHCEKEECDsrkwsIEAEFTLKLVSQNGK 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 18405153    104 G-KHKVHSHFDraleggpytlkyKGSMWGYKRFF 136
Cdd:smart00061  74 SlSKKDKHVFE------------KPSGWGFSKFI 95

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405153 194 CDIAFQVGD-ETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNVheitgstSASSF 272
Cdd:cd18302   6 YDVTIVSEDgKEFPCHKCVLVARLEYFHSMLSSSWIEASSCSALTMPIPSDILEIILDYLYTDEASAV-------KESQN 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18405153 273 TNMIQHLLAAADLYDLARLKILCEVLLCEKLDVDN 307
Cdd:cd18302  79 VEFLCNVLVIADQLLITRLKEICEVALVELLSLKN 113

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 18405153 303 LDVDNVATTLALAEQHQFLQLKAFCLEFVASPANlgAVMKSEGFKHLKQSCPTLLSE 359
Cdd:cd14821   1 LSVENAAEVLVLADLHSAEQLKTHAIDFINSHAT--DVMETEGWKSMVRSHPHLVAE 55

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 18405153 194 CDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLpNVHEitgstsassft 273
Cdd:cd18235  22 CDVILVADGVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDGKALLLLIDYVYTAEI-QVTE----------- 89

                        90       100       110
                ....*....|....*....|....*....|
gi 18405153 274 NMIQHLLAAADLYDLARLKILCevllCEKL 303
Cdd:cd18235  90 ENVQVLLPAANLLQLTDVRDAC----CDFL 115

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 18405153 184 LKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDvlpnvhei 263
Cdd:cd18360   1 LGLFFNSPLLADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTD-------- 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18405153 264 tGSTSASSFTNMiqHLLAAADLYDLARLKILCEVLLCEKL 303
Cdd:cd18360  73 -SCCPASILQAM--ALLICAEMYQVSRLQHICELYIITQL 109

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 18405153  29 FTIQGYSLAKgmSPGKFIQSDIFSVGGYDWAIYFYPDGKNpEDQSSYISLFIALASDSN-DIRALFELTLMDQSGKGKHK 107
Cdd:cd03773   9 FTLENFSTLR--QSADPVYSDPLNVDGLCWRLKVYPDGNG-EVRGNFLSVFLELCSGLGeASKYEYRVEMVHQANPTKNI 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18405153 108 VHShFDRALEggpytlkyKGSMWGYKRFFKRSALETSDYLKD--DCLVINCTV 158
Cdd:cd03773  86 KRE-FASDFE--------VGECWGYNRFFRLDLLINEGYLLPenDTLILRFSV 129