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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 179 LKVPECRLAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFV 258
Cdd:cd18343    1 LKVPECRLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 260267630 259 YTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18343   81 YTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCNNLSVEN 123

BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also termed HIB homolog 2, or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes containing homodimeric SPOPL or the heterodimer formed by speckle-type POZ protein (SPOP) and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 297 LSVENVADTLVLADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNNNQATDIMETSGWKSMIQSHPHLVAEAFRALAS 376
Cdd:cd18519    1 LSVENVADTLILADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNSNHATDIMETAGWKSMIHSHPHLVAEAFRALAS 80

                         90
                 ....*....|....*.
gi 260267630 377 SQCPQFGIPRKRLKQS 392
Cdd:cd18519   81 AQCPPFGIPRKRLKQS 96

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 260267630 179 LKVPECRLAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFV 258
Cdd:cd18343    1 LKVPECRLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 260267630 259 YTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18343   81 YTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCNNLSVEN 123

BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also termed HIB homolog 2, or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes containing homodimeric SPOPL or the heterodimer formed by speckle-type POZ protein (SPOP) and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 297 LSVENVADTLVLADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNNNQATDIMETSGWKSMIQSHPHLVAEAFRALAS 376
Cdd:cd18519    1 LSVENVADTLILADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNSNHATDIMETAGWKSMIHSHPHLVAEAFRALAS 80

                         90
                 ....*....|....*.
gi 260267630 377 SQCPQFGIPRKRLKQS 392
Cdd:cd18519   81 AQCPPFGIPRKRLKQS 96

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 260267630   201 DCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKMADNLLAAADKY 280
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 260267630   281 ALERLKVMCEEALCSNL 297
Cdd:smart00225  81 QIPGLVELCEEFLLKLL 97

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630    36 WTINNFSfcREEMGEVLKSSTFSSGpndKMKWCLRVNPKG--------LDDESKDYlslylllvscPKSEVRAKFKFSLL 107
Cdd:smart00061   4 HTFKNVS--RLEEGESYFSPSEEHF---NIPWRLKIYRKNgflslylhCEKEECDS----------RKWSIEAEFTLKLV 68

                           90       100       110
                   ....*....|....*....|....*....|
gi 260267630   108 NdkrEETKAMESQRAYRFVQGKDWGFKKFI 137
Cdd:smart00061  69 S---QNGKSLSKKDKHVFEKPSGWGFSKFI 95

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 260267630 179 LKVPECRLAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFV 258
Cdd:cd18343    1 LKVPECRLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 260267630 259 YTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18343   81 YTGKAPNLDKMADNLLAAADKYALERLKVMCEEALCNNLSVEN 123

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 260267630  28 KVVKFSYMWTINNFSFCREEMGEVLKSSTFSSGPNDKMKWCLRVNPKGLDDESKDYLSLYLLLVSCPKSEVRAKFKFSLL 107
Cdd:cd03774    1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSIL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260267630 108 NDKREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 166
Cdd:cd03774   81 NAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139

BACK (BTB and C-terminal Kelch) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also termed HIB homolog 2, or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes containing homodimeric SPOPL or the heterodimer formed by speckle-type POZ protein (SPOP) and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 297 LSVENVADTLVLADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNNNQATDIMETSGWKSMIQSHPHLVAEAFRALAS 376
Cdd:cd18519    1 LSVENVADTLILADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNSNHATDIMETAGWKSMIHSHPHLVAEAFRALAS 80

                         90
                 ....*....|....*.
gi 260267630 377 SQCPQFGIPRKRLKQS 392
Cdd:cd18519   81 AQCPPFGIPRKRLKQS 96

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 260267630 179 LKVPECRLAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFV 258
Cdd:cd18344    3 IKDPRHMLTDDLGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEERLKNPIEIHDLDPQVFKEMMGFI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 260267630 259 YTGKAPNLD--KMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18344   83 YTGKAPHLHshSMACDVLAAADKYGLEGLKVLCEDALCRNLSVEN 127

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 260267630  190 LGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKM 269
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENV 80

                          90       100
                  ....*....|....*....|....*...
gi 260267630  270 ADnLLAAADKYALERLKVMCEEALCSNL 297
Cdd:pfam00651  81 DD-LLAAADKLQIPSLVDKCEEFLIKSL 107

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        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260267630 297 LSVENVADTLVLADLHSAEQLKAQAIDFINRCsvlrqlgckdgknwnnnqATDIMETSGWKSMIQSHPHLVAEAFRA 373
Cdd:cd14821    1 LSVENAAEVLVLADLHSAEQLKTHAIDFINSH------------------ATDVMETEGWKSMVRSHPHLVAEAFRA 59

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 260267630 186 LAEDLGNLWENTRFTDCCFFV--RGKEFKAHKSVLAARSPVFNAMF-EHEMEECTKNRVEINDLDPEVFKEMMRFVYTGK 262
Cdd:cd18294    1 FAADMKSLINNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRAMFlTGPQKESTQSPLVLSDIEPEVFRAVLEFIYTNC 80

                         90       100
                 ....*....|....*....|....*....
gi 260267630 263 APNLDKMADNLLAAADKYALERLKVMCEE 291
Cdd:cd18294   81 VTLSNHTVIEVLAAAVEYGLDELRKLCER 109

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 260267630   201 DCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKMADNLLAAADKY 280
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 260267630   281 ALERLKVMCEEALCSNL 297
Cdd:smart00225  81 QIPGLVELCEEFLLKLL 97

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 260267630 196 NTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKMADNLLA 275
Cdd:cd18352   10 NATLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMRFIYTGSVDITNDIAKDLLR 89

                         90       100
                 ....*....|....*....|....*..
gi 260267630 276 AADKYALERLKVMCEEALCSNLSVENV 302
Cdd:cd18352   90 AADQYLLEGLKRLCEYTIAQDLTLENI 116

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 260267630 195 ENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGK-APNLDKMADnL 273
Cdd:cd18314    2 NDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQvTLSEENVLD-L 80

                         90
                 ....*....|....*.
gi 260267630 274 LAAADKYALERLKVMC 289
Cdd:cd18314   81 LMLASKYQVPDLEKLC 96

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8); BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 184 CRLAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYtGKA 263
Cdd:cd18286    2 SRLGKDLLQLFLNGEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVSFVLLFIY-GGV 80

                         90       100
                 ....*....|....*....|....*
gi 260267630 264 PNLDKMAD--NLLAAADKYALERLK 286
Cdd:cd18286   81 LDLPDDVNlgELLSLADMYGLDGLK 105

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a component of a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 causes autosomal-dominant retinitis pigmentosa. 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 260267630 185 RLAEDLG---NLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTG 261
Cdd:cd18237    4 LLADFMGvmnNMRKQKTLCDVILIVEGREIKAHRVVLAAASHFFHLMFTSNMTESKSSEVELKDAEPDIIELLVEFAYTA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 260267630 262 KAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18237   84 RISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQLDASN 123

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 21 (KLHL21); KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 also targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 190 LGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKM 269
Cdd:cd18250   12 LSELRAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMFAGELRESRADRVVLHGVSAEILGLLLDFSYTGRVTVTQDN 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 260267630 270 ADNLLAAADKYALERLKVMCEEALCSNLSVENV 302
Cdd:cd18250   92 VEALLRAADLFQFPSVKEACCAYLQQRLDVSNC 124

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 260267630 185 RLAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAmfeheMEECTKNRVEINDLDPEVFKEMMRFVYTGKAP 264
Cdd:cd18303    4 RLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSN-----ENLASTNELDLSDISYEVVLALLRWLYTDELD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 260267630 265 nlDKMADN----LLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18303   79 --LTLDDEflleLMKAAKRFQLTDLVERCERALMSSVNVDN 117

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 30 (KLHL30); KLHL30 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260267630 188 EDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGK 262
Cdd:cd18259   21 DGLQTLRSNPKLSDVTLLVGGREFPCHRSVLALCSHYFNAMFTGDFVESISARVEIKDVDPAVMESLIDFAYTGK 95

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 260267630 190 LGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGK-APNLDK 268
Cdd:cd18255    9 LNALRAKGQLLDVTLIADGQRFQAHKVVLASCSDYFRAMFTGGMRESSQDEIELKGVSAKGLKHILDFAYTSElTLDLDC 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 260267630 269 MADnLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18255   89 IQD-VLGAAVHLQMLPVVELCEEFLKSAMSVEN 120

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 260267630 188 EDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKapnLD 267
Cdd:cd18306    7 AKLNALRKNRQFCDVILQVGGHEIPAHRAVLACASPYLFELFSSDSDGESILTVKLDGLDPDAVEVLVNYAYTSR---LE 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 260267630 268 KMAD---NLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18306   84 VPADlvkSVYSAAKKLKMDRVKKACGDFLLEKLTPQN 120

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 260267630 186 LAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPN 265
Cdd:cd18269   14 LQDGLKDLLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEIDL 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 260267630 266 LDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18269   94 NDQNVQDIFALASRFQIPSIFTVCVSYLQKRLSLSN 129

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 260267630 196 NTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKMADNLLA 275
Cdd:cd18240   14 EGKLCDVVIRVNGVEFPAHRNILCACSPYFRALFTNGWNETEKKVYKIPGVSPEMMELIIEYAYTRTVPITAENVEELLP 93

                         90       100
                 ....*....|....*....|....*.
gi 260267630 276 AADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18240   94 AADQFNIMGIVKACCDFLEDQLCPEN 119

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like ECH-associated protein 1 (KEAP1); KEAP1, also called cytosolic inhibitor of Nrf2 (INrf2) or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260267630 209 KEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTG 261
Cdd:cd18248   35 EEFMAHKVVLASSSPYFKAMFTSGLRECGMEVVPIEGVHPCVMSRLIEFAYTA 87

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 260267630 186 LAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHE--MEECTKNRVEINDLDPEVFKEMMRFVYTGKA 263
Cdd:cd18245    1 LLRALNSFREEPHLCDATLVVGGEEIPVQKNVLAAASPYFRAKLNYNppKDDGSTYKIELEGISVEVMEEILDYIYTGQI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 260267630 264 P-NLDKMADnLLAAADKYALERLKVMCEEAL 293
Cdd:cd18245   81 KlSEDNIQD-IVQAADLLLMTDLKDLCCEFL 110

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 260267630 182 PECRLAEdLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEIND-LDPEVFKEMMRFVYT 260
Cdd:cd18254    6 PDCVLTH-LNTLRKQCMFTDVTLWAGNRSFPCHRAVLAACSRYFEAMFSNGLRESLDSTVNFHDsLHPEVLELLLDFAYS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 260267630 261 GKAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18254   85 SRIIINEENAESLLEAGDMLQFHDVRDAAAEFLEKNLYPSN 125

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 260267630 208 GKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKMADNLLAAADKYALERLKV 287
Cdd:cd18235   30 GVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDGKALLLLIDYVYTAEIQVTEENVQVLLPAANLLQLTDVRD 109

                         90
                 ....*....|
gi 260267630 288 MCEEALCSNL 297
Cdd:cd18235  110 ACCDFLQSQL 119

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 260267630 208 GKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPNLDKMADNLLAAADKYALERLKV 287
Cdd:cd18273   43 GRLFPCNRNVLAAASPYFKSMFTGGLYESKQETVTIHDVDSESMALIIDYCYTGRVTLSEANVQRLYAAANMLQLEYVRE 122

                         90
                 ....*....|....*....
gi 260267630 288 MCEEALCSNLSVENVADTL 306
Cdd:cd18273  123 ACASFLARRLDLSNCVGIL 141

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 2 (KBTBD2); KBTBD2, also called BTB and kelch domain-containing protein 1 (BKLHD1), plays an essential role in the regulation of insulin-signaling pathway. It is a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase, which targets p85alpha, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85alpha ubiquitination and proteasome-mediated degradation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260267630 186 LAEDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMEECTKNRVEINDLDPEVFKEMMRFVYTGKAPN 265
Cdd:cd18270   13 LLEQLKFFYEQQLLTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAATLQIIITYAYTGNLAI 92

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 260267630 266 LDKMADNLLAAADKYALERLKVMCEEALCSNLSVEN 301
Cdd:cd18270   93 NDSTVEQLYETACFLQVEDVLQRCREYLIKKINAEN 128

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260267630 188 EDLGNLWENTRFTDCCFFVRGKEFKAHKSVLAARSPVFNAMFEHEMeectKNRVEIN----DLDPEVFKEMMRFVYTG 261
Cdd:cd18295    8 EFLRRLLEQGSYSDVTFNVHGESFPAHRCILSARSPYFAEMFETKW----KDKREINlkhpLVNPDAFRALLQYLYTG 81