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 71990953  50 KVVKFNYMWTINNFSFCREEMGEVLKSSTFSAGCNDKLKWCLRINPKGLDEESRDYLSLYLLLVQCNKSEVRAKFKFSIL 129
Cdd:cd03774   1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990953 130 NAKREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPGDRLSIFCEVSVVAE 188
Cdd:cd03774  81 NAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139

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 71990953 326 LTTDNASLTLMLADMYSASQLRAHSINFINVNANEVMDTEGWEDLVRDHPKLLEEVFRA 384
Cdd:cd14821   1 LSVENAAEVLVLADLHSAEQLKTHAIDFINSHATDVMETEGWKSMVRSHPHLVAEAFRA 59

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 71990953  50 KVVKFNYMWTINNFSFCREEMGEVLKSSTFSAGCNDKLKWCLRINPKGLDEESRDYLSLYLLLVQCNKSEVRAKFKFSIL 129
Cdd:cd03774   1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990953 130 NAKREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPGDRLSIFCEVSVVAE 188
Cdd:cd03774  81 NAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139

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 71990953   213 MYGLFDNKQFSDFTLVCKsdlgspTQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQT 292
Cdd:pfam00651   1 LNELREQGELCDVTLVVG------DKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKL 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 71990953   293 KYiEQMAQSLIAAADKYQLDRLKVMCEQALCYQL 326
Cdd:pfam00651  75 IS-EENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990953    224 DFTLVCKSdlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQMAQSLI 303
Cdd:smart00225   1 DVTLVVGG------KKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELL 74

                           90       100
                   ....*....|....*....|...
gi 71990953    304 AAADKYQLDRLKVMCEQALCYQL 326
Cdd:smart00225  75 ELADYLQIPGLVELCEEFLLKLL 97

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 71990953    60 INNFSfcREEMGEVLKSSTFSAGcndKLKWCLRINPKGldeesrDYLSLYLllvQCNKSE-------VRAKFKFSILNAK 132
Cdd:pfam00917   1 IKNFS--KIKEGESYYSPVEERF---NIPWRLQIYRKG------GFLGLYL---HCDKEEelergwsIETEFTLKLVSSN 66

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 71990953   133 ReetKAMESQRAYRFVQGKDWGFKKFIRRDFLLDE 167
Cdd:pfam00917  67 G---KSVTKTDTHVFEKPKGWGWGKFISWDDLEKD 98

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 71990953  50 KVVKFNYMWTINNFSFCREEMGEVLKSSTFSAGCNDKLKWCLRINPKGLDEESRDYLSLYLLLVQCNKSEVRAKFKFSIL 129
Cdd:cd03774   1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990953 130 NAKREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPGDRLSIFCEVSVVAE 188
Cdd:cd03774  81 NAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139

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 71990953 205 PPCRLADDMYGLFDNKQFSDFTLvCKSDlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELL 284
Cdd:cd18345   1 PECRLSDDLGLLFERSAFSDVTL-CVGG-----REFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVMREML 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71990953 285 VYMYTGQTKYIEQMAQSLIAAADKYQLDRLKVMCEQALCYQLTTDNA 331
Cdd:cd18345  75 RFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEEALCSNLSVENV 121

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 71990953 201 LFKVPPCRLADDMYGLFDNKQFSDFTLVCKSdlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVM 280
Cdd:cd18342   1 MVKVPECRLADELGGLWENSRFTDCCLCVAG------QEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVF 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71990953 281 RELLVYMYTGQTKYIEQMAQSLIAAADKYQLDRLKVMCEQALCYQLTTDNA 331
Cdd:cd18342  75 KEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENA 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 71990953   213 MYGLFDNKQFSDFTLVCKsdlgspTQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQT 292
Cdd:pfam00651   1 LNELREQGELCDVTLVVG------DKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKL 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 71990953   293 KYiEQMAQSLIAAADKYQLDRLKVMCEQALCYQL 326
Cdd:pfam00651  75 IS-EENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107

BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein roadkill and similar proteins; 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        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990953 326 LTTDNASLTLMLADMYSASQLRAHSINFINVNANEVMDTEGWEDLVRDHPKLLEEVFRALATQQTPPvvlVQPPKKR 402
Cdd:cd18520   1 LSVETAAEVLILADLHSADQLKAQAIDFINTHATDVMETAGWKSMIRTHPHLLAEAFRALATQQIPP---IGPPRKR 74

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 71990953  56 YMWTINNFSfcrEEMGEVLKSSTFSAGcndKLKWCLRINPKGlDEESRDYLSLYLLLVQC----NKSEVRAKFKFSILNA 131
Cdd:cd00121   3 HTWKIVNFS---ELEGESIYSPPFEVG---GYKWRIRIYPNG-DGESGDYLSLYLELDKGesdlEKWSVRAEFTLKLVNQ 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 71990953 132 KREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANglLPGDRLSIFCEV 183
Cdd:cd00121  76 NGGKSLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYY--LVDDSLTIEVEV 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 71990953 209 LADDMYGLFDNKQFSDFTLVCKSdlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMY 288
Cdd:cd18280   1 LGQHFGALLESEEGADVTFNVDG------EKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVFKALLHFIY 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71990953 289 T------------GQTKYIEQMAQSLIAAADKYQLDRLKVMCEQALC 323
Cdd:cd18280  75 KdelpddvepagsDSSSLDTTMAQHLLAAADRYALERLRLLCESRLC 121

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 71990953 217 FDNKQFSDFTLVCKsdlgspTQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIE 296
Cdd:cd18314   1 YNDSEFSDVVLCVG------DRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQVTLSE 74

                        90       100
                ....*....|....*....|..
gi 71990953 297 QMAQSLIAAADKYQLDRLKVMC 318
Cdd:cd18314  75 ENVLDLLMLASKYQVPDLEKLC 96

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 23 (KLHL23); KLHL23 overexpression is associated with increased cell proliferation and invasion in gastric cancer. Downregulation of KLHL23 is associated with invasion, metastasis, and poor prognosis of hepatocellular carcinoma and pancreatic cancer. KLHL23 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 71990953 222 FSDFTLVCKSDlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQMAQS 301
Cdd:cd18252  21 FTDITLQCASG-----QIFHCHKAALAACSSYFKVMFTADMKEKSNNVIKLSGIDHDILEALVNYVYTSQICITERNVQS 95

                        90       100
                ....*....|....*....|....*....
gi 71990953 302 LIAAADKYQLDRLKVMCEQALCYQLTTDN 330
Cdd:cd18252  96 LLEAADLLQFISVKKACEQFLVRHLDIDN 124

BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein (SPOP); SPOP, also termed HIB homolog 1, or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of 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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990953 326 LTTDNASLTLMLADMYSASQLRAHSINFINVNANEVMDTEGWEDLVRDHPKLLEEVFRALATQQTPpvvLVQPP 399
Cdd:cd18518   1 LSVENAAEILILADLHSADQLKTQAVDFINYHASDVMETSGWKSMVVSHPHLVAEAYRSLASAQCP---FLGPP 71

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 71990953 216 LFDNKQFSDFTLVCKSdlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYI 295
Cdd:cd18297   6 YVNNPEMSDVTFLVEG------RPFYAHKIVLVTASDRFKSMLSSGSTEAQTPVIEIPDIRYDIFQLMMQYLYTGGVESL 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71990953 296 EQM---AQSLIAAADKYQLDRLKVMCEQALCYQLTTDN 330
Cdd:cd18297  80 DVAqddALELLRAASFFQLDGLKRHCEILLSQQIDLDN 117

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 71990953 238 QTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQMAQSLIAAADKYQLDRLKVM 317
Cdd:cd18256  30 ELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPDIFHILLDFIYTGVVEVTVSNVQELLVAADMLQLTEVVEI 109

                        90
                ....*....|....
gi 71990953 318 CEQALCYQLTTDNA 331
Cdd:cd18256 110 CCEFLKGQLHPSNC 123

BACK (BTB and C-terminal Kelch) domain found in TD and POZ domain-containing proteins, Tdpoz1-4; 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 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)", and are not inlcuded in this subfamily.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990953 326 LTTDNASLTLMLADMYSASQLRAHSINFINVNANEVMDTEGWEDLVRDHPKLLEEVFRALATQQ 389
Cdd:cd18521   1 LSVKNAAHTLILADLHSTEKLKTQALDFIAVHASEVSETSEWKSMVESHPHLVAEAFHSLASAQ 64

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing proteins KBTBD6 and KBTBD7; KBTBD6 and KBTBD7 are substrate adaptors of a cullin-3 RING ubiquitin ligase complex that mediates ubiquitylation and proteasomal degradation of T-lymphoma and metastasis gene 1 (TIAM1), a RAC1-specific guanine exchange factor (GEF), by cooperating with gamma-aminobutyric acid receptor-associated proteins (GABARAP). KBTBD7 may also act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling. They both contain a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990953 209 LADDMYGLFDNKQFSDFTL--VCKSDLGSPTQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVY 286
Cdd:cd18273  13 LLAQLKSFYDARLLTDVTIevNGPGSGPGSGRLFPCNRNVLAAASPYFKSMFTGGLYESKQETVTIHDVDSESMALIIDY 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71990953 287 MYTGQTKYIEQMAQSLIAAADKYQLDRLKVMCEQALCYQLTTDN 330
Cdd:cd18273  93 CYTGRVTLSEANVQRLYAAANMLQLEYVREACASFLARRLDLSN 136

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 71990953 218 DNKQFSDFTLVCKSdlgsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVD--DIEPEVMRELLVYMYTGQTKYI 295
Cdd:cd18245  10 EEPHLCDATLVVGG------EEIPVQKNVLAAASPYFRAKLNYNPPKDDGSTYKIEleGISVEVMEEILDYIYTGQIKLS 83

                        90       100
                ....*....|....*....|...
gi 71990953 296 EQMAQSLIAAADKYQLDRLKVMC 318
Cdd:cd18245  84 EDNIQDIVQAADLLLMTDLKDLC 106

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 10 (KLHL10); KLHL10 is a substrate-specific adaptor of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins specifically in the testis during spermatogenesis. Haploinsufficiency of Klhl10 causes infertility in male mice. KLHL10 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990953 238 QTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQMAQSLIAAADKYQLDRLKVM 317
Cdd:cd18240  27 VEFPAHRNILCACSPYFRALFTNGWNETEKKVYKIPGVSPEMMELIIEYAYTRTVPITAENVEELLPAADQFNIMGIVKA 106

                        90
                ....*....|...
gi 71990953 318 CEQALCYQLTTDN 330
Cdd:cd18240 107 CCDFLEDQLCPEN 119

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990953     58 WTINNFSfcREEMGEVLKSSTFSAGcndKLKWCLRINPKGldeesrDYLSLYLllvQCNKSE-------VRAKFKFSILN 130
Cdd:smart00061   4 HTFKNVS--RLEEGESYFSPSEEHF---NIPWRLKIYRKN------GFLSLYL---HCEKEEcdsrkwsIEAEFTLKLVS 69

                           90       100
                   ....*....|....*....|....*....
gi 71990953    131 AkreETKAMESQRAYRFVQGKDWGFKKFI 159
Cdd:smart00061  70 Q---NGKSLSKKDKHVFEKPSGWGFSKFI 95

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 8 (KBTBD8); KBTBD8, also called T-cell activation kelch repeat protein (TA-KRP), is a BTB-kelch family protein that is located in the Golgi apparatus and translocates to the spindle apparatus during mitosis. It acts as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex monoubiquitylates NOLC1 and its paralog TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome. 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 71990953 207 CRLADDMYGLFDNKQFSDftLVCKSDLGsptQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVY 286
Cdd:cd18274   7 CSILQQLKAMYDEGQLTD--IVVEVDHG---KTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGVEAESMHLVLDY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71990953 287 MYTGQTKYIEQMAQSLIAAADKYQLDRLKVMCEQALCYQLTTDNA 331
Cdd:cd18274  82 AYTSRVTLTEANVQALFTAASIFQIPSLQDQCAQFMISRLDPQNS 126

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as a substrate-specific adaptor for a Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990953 238 QTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQMAQSLIAAADKYQLDRLKVM 317
Cdd:cd18247  29 QKFSAHRIVLAATIPYFHAMFTHDMVESKQDEITMQGIEPSALEALINFAYSGRIAIDTSNVQSLLVGASFLQLQSVKDA 108

                .
gi 71990953 318 C 318
Cdd:cd18247 109 C 109

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 32 (KLHL32); KLHL32, also called BTB and kelch domain-containing protein 5 (BKLHD5), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Deletion of KLHL32 may be ssociated with Tourette syndrome and obsessive-compulsive disorder. 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 71990953 219 NKQFSDfTLVCKSDLGSPTQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQM 298
Cdd:cd18261  20 NQQRND-GILCDITLVAEEQKFHAHKAVLAACSDYFRAMFSLCMVESEADEVNLHGVTSLGLKQALDFAYTGQILLEPGV 98

                        90       100       110
                ....*....|....*....|....*....|..
gi 71990953 299 AQSLIAAADKYQLDRLKVMCEQALCYQLTTDN 330
Cdd:cd18261  99 IQDVLAAGSHLQLLELLSLCSHYLIQELNSFN 130

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 25 (KLHL25); KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that is required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1). Cullin3-KLHL25 ubiquitin ligase also targets ATP-citrate lyase (ACLY), a key enzyme for lipid synthesis, for degradation to inhibit lipid synthesis and tumor progression. KLHL25 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 71990953 222 FSDFTLvcksdlGSPTQTFHIHKAILAARSRVFSAMFEHHMQES-DTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQMAQ 300
Cdd:cd18254  22 FTDVTL------WAGNRSFPCHRAVLAACSRYFEAMFSNGLRESlDSTVNFHDSLHPEVLELLLDFAYSSRIIINEENAE 95

                        90
                ....*....|.
gi 71990953 301 SLIAAADKYQL 311
Cdd:cd18254  96 SLLEAGDMLQF 106

first 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, tandem BTB domains, and a conserved C-terminal region. In vertebrates, 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 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 71990953 211 DDMYGLFDNKQFSDFTLVCKSDlgsptQTFHIHKAILAARSRVFSAMFehhmqesdTNMTTV---DDIEPEVMRELLVYM 287
Cdd:cd18299   1 EDLRNLLHSPSCADVVFILQGG-----VRIFAHRIVLAAASSVFADLF--------LMMTVVtldSDITPEAFRRVLEFL 67

                        90       100       110
                ....*....|....*....|....*....|..
gi 71990953 288 YTGQTKYIEQMAQSLIAAADKYQLDRLKVMCE 319
Cdd:cd18299  68 YTGVLDENEDDLKELKDAAELLELFDLVMMCT 99

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990953 219 NKQFSDFTLVCKsdlgspTQTFHIHKAILAARSRVFSAMFEHHMQESDTNMTTVDDIEPEVMRELLVYMYTGQTKYIEQM 298
Cdd:cd18306  15 NRQFCDVILQVG------GHEIPAHRAVLACASPYLFELFSSDSDGESILTVKLDGLDPDAVEVLVNYAYTSRLEVPADL 88

                        90       100       110
                ....*....|....*....|....*....|...
gi 71990953 299 AQSLIAAADKYQLDRLKVMCEQALCYQLTTDNA 331
Cdd:cd18306  89 VKSVYSAAKKLKMDRVKKACGDFLLEKLTPQNC 121