first 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 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 755545647 102 EASHYHSDLNNLLLCCQCVDVVFYHPEVTGVVEAHKIVLCSVSHVFMLLFNVKSPADIQDSSIIRTTQDLFAINRDAVLP 181
Cdd:cd18357    1 EASHYNSDLLNLLYSCQCADVAFCTEDLKEVGEAHRVVLCSVSQVFMLLFGVKSTREIQDSSIGRTAQSLFAVDGDDIFP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545647 182 GASQEAPSN-PPLPVIVKDALFCSCLSDILRFIYSGAFQWEELEEDVRRKLKDSGDVSDIIEKVKCILKTPGKINCLRN 259
Cdd:cd18357   81 APSHDLHTAgPPVRVIVKDSLLCACLPEILKFIYSGASQWEELEEDLRKKLKDSEKVEHVLEKVKCLLKTPGKLRCLRD 159

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. RhoBTB3 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) by facilitating hydroxylation and ubiquitination.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545647 395 MNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRKCRC 474
Cdd:cd18532    1 TSLSVVSLLRKAKFHNADQLSTWLLHFIASNYLIFSQKPEFQDLSAEERDFVETHRWPSSMYLQELAEYRQHIHSRKSRC 80

                 ...
gi 755545647 475 LVM 477
Cdd:cd18532   81 SVM 83

first 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 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 755545647 102 EASHYHSDLNNLLLCCQCVDVVFYHPEVTGVVEAHKIVLCSVSHVFMLLFNVKSPADIQDSSIIRTTQDLFAINRDAVLP 181
Cdd:cd18357    1 EASHYNSDLLNLLYSCQCADVAFCTEDLKEVGEAHRVVLCSVSQVFMLLFGVKSTREIQDSSIGRTAQSLFAVDGDDIFP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545647 182 GASQEAPSN-PPLPVIVKDALFCSCLSDILRFIYSGAFQWEELEEDVRRKLKDSGDVSDIIEKVKCILKTPGKINCLRN 259
Cdd:cd18357   81 APSHDLHTAgPPVRVIVKDSLLCACLPEILKFIYSGASQWEELEEDLRKKLKDSEKVEHVLEKVKCLLKTPGKLRCLRD 159

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. RhoBTB3 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) by facilitating hydroxylation and ubiquitination.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545647 395 MNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRKCRC 474
Cdd:cd18532    1 TSLSVVSLLRKAKFHNADQLSTWLLHFIASNYLIFSQKPEFQDLSAEERDFVETHRWPSSMYLQELAEYRQHIHSRKSRC 80

                 ...
gi 755545647 475 LVM 477
Cdd:cd18532   81 SVM 83

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 755545647   287 DVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAgIFQAMCLLICAEM 366
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLP-EENVEELLELADY 79

                           90
                   ....*....|....*...
gi 755545647   367 YQVSRLQHICELFIITQL 384
Cdd:smart00225  80 LQIPGLVELCEEFLLKLL 97

first 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 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 755545647 102 EASHYHSDLNNLLLCCQCVDVVFYHPEVTGVVEAHKIVLCSVSHVFMLLFNVKSPADIQDSSIIRTTQDLFAINRDAVLP 181
Cdd:cd18357    1 EASHYNSDLLNLLYSCQCADVAFCTEDLKEVGEAHRVVLCSVSQVFMLLFGVKSTREIQDSSIGRTAQSLFAVDGDDIFP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545647 182 GASQEAPSN-PPLPVIVKDALFCSCLSDILRFIYSGAFQWEELEEDVRRKLKDSGDVSDIIEKVKCILKTPGKINCLRN 259
Cdd:cd18357   81 APSHDLHTAgPPVRVIVKDSLLCACLPEILKFIYSGASQWEELEEDLRKKLKDSEKVEHVLEKVKCLLKTPGKLRCLRD 159

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. RhoBTB3 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) by facilitating hydroxylation and ubiquitination.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545647 395 MNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRKCRC 474
Cdd:cd18532    1 TSLSVVSLLRKAKFHNADQLSTWLLHFIASNYLIFSQKPEFQDLSAEERDFVETHRWPSSMYLQELAEYRQHIHSRKSRC 80

                 ...
gi 755545647 475 LVM 477
Cdd:cd18532   81 SVM 83

BACK (BTB and C-terminal Kelch) 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 C-terminal BACK domain. 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755545647 395 MNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIF-SQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIH 468
Cdd:cd18499    1 IDEDVIDLLELAQLHNADQLAAWCLHFISTNYNAFcKHRKEFKLLSPENQEYIEEHRWPPVWYLKELDEYEKKLK 75

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 755545647  279 FLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGifQAM 358
Cdd:pfam00651   4 LREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEE--NVD 81

                          90       100
                  ....*....|....*....|....*.
gi 755545647  359 CLLICAEMYQVSRLQHICELFIITQL 384
Cdd:pfam00651  82 DLLAAADKLQIPSLVDKCEEFLIKSL 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 755545647   287 DVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAgIFQAMCLLICAEM 366
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLP-EENVEELLELADY 79

                           90
                   ....*....|....*...
gi 755545647   367 YQVSRLQHICELFIITQL 384
Cdd:smart00225  80 LQIPGLVELCEEFLLKLL 97

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 755545647 272 YNTSLKFFLNKPMLADVVFEI--QGATVPAHRAILVARCEVMAAMFN-GNYMEAKSVLIPVYGVSKETFLSFLEYLYTDs 348
Cdd:cd18294    1 FAADMKSLINNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRAMFLtGPQKESTQSPLVLSDIEPEVFRAVLEFIYTN- 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755545647 349 CCPAGIFQAMCLLICAEMYQVSRLQHICELFI 380
Cdd:cd18294   80 CVTLSNHTVIEVLAAAVEYGLDELRKLCERFI 111

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 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. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. 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 755545647 261 KTYQARKPlwfynTSLKFFLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSF 340
Cdd:cd18358    1 KAFHVRKA-----NRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755545647 341 LEYLYTDSCCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQL 384
Cdd:cd18358   76 LDYLYTKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQEL 119

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in armadillo repeat-containing protein 5 (ARMC5); ARMC5 plays a role in steroidogenesis, and modulates the expression and cortisol production of steroidogenic enzymes. It negatively regulates adrenal cells survival. It contains armadillo (ARM) repeats and a BTB domain, which is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545647 286 ADVVFEIQ-GATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLY--TDSCCPAG 353
Cdd:cd18191    2 HDLRFLLDgGTQLPASRAALTGASEVFRAMLEGGFAEAQQDLVPLRQVPSGAFLPVLHYLHgcRGCDANED 72

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2; The RCC1-related guanine nucleotide exchange factor (GEF) family includes RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2, both of which are chromosome condensation regulator-like guanine nucleotide exchange factors. They contain an RCC1 repeat, a BTB domain, and a BACK 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 755545647 274 TSLKFFLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAG 353
Cdd:cd18298    1 DSLRKAFNDPRTSDLKFRVDGKYIYVHKAILKIRCEYFRSMFQSHWNEDDKNVIEIDQYSYPVYYAFLRYLYTDQVDLPP 80

                         90       100
                 ....*....|....*....|....*..
gi 755545647 354 IfQAMCLLICAEMYQVSRLQHICELFI 380
Cdd:cd18298   81 E-DAIGLLDLANSYCEERLKKLCEDII 106

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1); RCBTB1 is also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), CLL deletion region gene 7 protein, regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5. It is a novel chromosome condensation regulator-like guanine nucleotide exchange factor that may be involved in cell cycle regulation by chromatin remodeling. It may also function as a tumor suppressor that regulates pathways of DNA damage/repair and apoptosis. RCBTB1 may also be a substrate adaptor for a cullin3 (CUL3) E3 ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Biallelic mutations in RCBTB1 may cause isolated and syndromic retinal dystrophy. It contains an RCC1 repeat, a BTB domain, and a BACK 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 755545647 275 SLKFFLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSC-CPAG 353
Cdd:cd18353   10 SLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYPVYRAFLEYLYTDSVdLPPE 89

                         90       100
                 ....*....|....*....|....*..
gi 755545647 354 ifQAMCLLICAEMYQVSRLQHICELFI 380
Cdd:cd18353   90 --DAIGLLDLATSYCENRLKKLCQHII 114

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. RhoBTB1 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545647 398 DIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQK--PEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRK 471
Cdd:cd18530    4 EVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKfrKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKERE 79

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2); RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2), or p83, is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. RhoBTB2 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755545647 398 DIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQK--PEFQDLSVEERSFVEKHRWPSNMYLKqlaEYRKYIHSRKCR 473
Cdd:cd18531    4 QVLVYLELAQFHNAKQLADWCLHHICTNYNSVCRKfpRDMKAMSPENQEHFEKHRWPPVWYLK---EEDRYLRSKKER 78

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing protein 2 (RCBTB2); RCBTB2 is also called chromosome condensation 1-like (CHC1-L), RCC1-like G exchanging factor, or regulator of chromosome condensation and BTB domain-containing protein 2. It is a chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) protein for the Ras-related GTPase Ran. It contains an RCC1 repeat, a BTB domain, and a BACK 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 755545647 275 SLKFFLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEaksvLIPVYGVSKETFLSFLEYLYTDSCCPAGi 354
Cdd:cd18354   10 SLKREFDNPDTADLKFLVDGKYIYVHKVLLKIRCEHFRSLLNENEEE----IIEMSQFSYPVYRAFLEYLYTDSISLSP- 84

                         90       100
                 ....*....|....*....|...
gi 755545647 355 FQAMCLLICAEMYQVSRLQHICE 377
Cdd:cd18354   85 EDAIGLLDLATFYRENRLKKLCQ 107

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 1 (BTBD1); BTBD1, also called Hepatitis C virus NS5A-transactivated protein 8 or HCV NS5A-transactivated protein 8, is a BTB-domain-containing Kelch-like protein that is expressed in skeletal muscle and interacts 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. BTBD1 may serve as substrate-specific adaptor of an E3 ubiquitin-protein ligase complex that 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 755545647 278 FFLNKPMLADVVFEI----------QGATVPAHRAILVARCEVMAAMFNGNyMEAKSVLIPVYGVSKETFLSFLEYLYTD 347
Cdd:cd18346   15 FLFNNELLSDVRFVVgkgrprgpgpGAQRIPAHRFVLAAGSAVFDAMFNGG-MATTSAEIELPDVEPAAFLALLRFLYSD 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755545647 348 ScCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQS 386
Cdd:cd18346   94 E-VQIGPETVMTTLYTAKKYAVPALEAHCVEFLTKHLRA 131

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 755545647 287 DVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTdSCCPAGIFQAMCLLICAEM 366
Cdd:cd18256   22 DVQLQVGMELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPDIFHILLDFIYT-GVVEVTVSNVQELLVAADM 100

                         90       100
                 ....*....|....*....|
gi 755545647 367 YQVSRLQHICELFIITQLQS 386
Cdd:cd18256  101 LQLTEVVEICCEFLKGQLHP 120

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545647 280 LNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDS 348
Cdd:cd18295   14 LEQGSYSDVTFNVHGESFPAHRCILSARSPYFAEMFETKWKDKREINLKHPLVNPDAFRALLQYLYTGR 82

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; This family contains the Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. Family members 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 755545647 285 LADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTdsccpaGIFQ-----AMC 359
Cdd:cd18234    1 LCDVILIAGDRRIPAHRLVLSAVSDYFAAMFTNDVREATEEEIKLKDVDPDALWTLVQYCYT------GRLElkednVES 74

                         90       100
                 ....*....|....*....|....*
gi 755545647 360 LLICAEMYQVSRLQHICELFIITQL 384
Cdd:cd18234   75 LLATACLLQLSEVVEACCGFLMKQL 99

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 4 (KLHL4); KLHL4 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It may be associated with X-linked cleft palate (CPX) and is also a candidate gene in the impairment of mullerian duct development. In addition, it has been identified as a target of insulin-like growth factor binding protein 5 (IGFBP5). KLHL4 contains 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 755545647 279 FLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTdsccpaGIFQAM 358
Cdd:cd18336   13 YLQHKQLCDVLLIAGNLKIPAHRLVLSAVSDYFAAMFTNDVREAKQEEIKMEGVDPDALKALVHYAYT------GVLELK 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755545647 359 -----CLLICAEMYQVSRLQHICELFIITQLQ 385
Cdd:cd18336   87 edtieSLLAAACLLQLSQVIDVCCNFLMKQLH 118

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 6 (BTBD6); BTBD6, also termed lens BTB domain protein, is a BTB-domain-containing Kelch-like protein required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545647 280 LNKPMLADVVFEI--QGAT--VPAHRAILVARCEVMAAMFNGNYMEAKS-VLIPvyGVSKETFLSFLEYLYTDSCCPAGI 354
Cdd:cd18349    3 FNNELMADVHFIVgpPGASqrVPAHKYVLAVGSSVFYAMFYGDLAEVKSeIHIP--DVEPAAFLILLKYMYSDEIDLEAD 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 755545647 355 fQAMCLLICAEMYQVSRLQHICELFIITQL 384
Cdd:cd18349   81 -TVLATLYAAKKYIVPALAKACVNFLETSL 109

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 2 (BTBD2); BTBD2 is a BTB-domain-containing Kelch-like protein that interacts 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545647 263 YQARKPLwfYNTSLKFFLNKPMLADVVFEIQGAT----VPAHRAILVARCEVMAAMFNGNyMEAKSVLIPVYGVSKETFL 338
Cdd:cd18347    2 WQATKPT--VQERFAFLFNNEVLSDVHFLVGKGLgsqrIPAHRFVLAVGSAVFDAMFNGG-MATTSTEIELPDVEPAAFL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755545647 339 SFLEYLYTDScCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQS 386
Cdd:cd18347   79 ALLKFLYSDE-VQIGPETVMTTLYTAKKYAVPALEAHCVEFLKKNLRA 125

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 755545647 285 LADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYT-DSCCPAGIFQAmcLLIC 363
Cdd:cd18237   21 LCDVILIVEGREIKAHRVVLAAASHFFHLMFTSNMTESKSSEVELKDAEPDIIELLVEFAYTaRISVNSNNVQS--LLDA 98

                         90       100
                 ....*....|....*....|.
gi 755545647 364 AEMYQVSRLQHICELFIITQL 384
Cdd:cd18237   99 ANQYQIEPVKKMCVDFLKEQL 119

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 755545647 286 ADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSccpAGIFQAMC--LLIC 363
Cdd:cd18279   19 TDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGK---APNLDKMAddLLAA 95

                         90
                 ....*....|....
gi 755545647 364 AEMYQVSRLQHICE 377
Cdd:cd18279   96 ADKYALERLKVMCE 109

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 35 (KLHL35); KLHL35 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Significant differences in DNA methylation of the KLHL35 gene in abdominal aortic aneurysm (AAA) patients compared to non-AAA controls suggest a potential role in AAA pathology. Hypermethylation of the KLHL35 gene has also been associated with the development of hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545647 285 LADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCC-----PAGIFQAmc 359
Cdd:cd18265   23 FTDVVLLVDGKDFPCHRATLSANSAYFRAMFGGHLKESRQAVVEIQKVSAAAMEVLLDYMYGGGLRiqednVESVLEA-- 100

                         90       100
                 ....*....|....*....|....*
gi 755545647 360 llicAEMYQVSRLQHICELFIITQL 384
Cdd:cd18265  101 ----SDLLQVSKLREACVRFLEGQL 121

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 22 (KLHL22); KLHL22 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of polo-like kinase 1 (PLK1) at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates mono-ubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755545647 284 MLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYT 346
Cdd:cd18251   22 ILFDVVLVVEGKPIEAHRILLAASCDYFRGMFAGGLREMQQTEVLIHGVSYNAMCKILDFIYT 84

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755545647 287 DVVFEIQGATVPAHRAILVARCEVMAAMF-NGNYMEAKSVLIPVYGVSK---ETFLSFLEYLYTDSC 349
Cdd:cd18301   20 DVVFQVGGKTFPAHKFILASRSDYFRKLFlSSLLTSEDAVGCDVVHIEKvppEIFEQLLQFIYTDTC 86

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 3 (KLHL3); KLHL3 is a component of an E3 ubiquitin ligase complex that regulates blood pressure by targeting With-No-Lysine (WNK) kinases for degradation. It contains 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 755545647 281 NKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTdscCPAGIFQ--AM 358
Cdd:cd18339   17 SKQLLCDVTIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYT---AEIEVTEenVQ 93

                         90       100
                 ....*....|....*....|....*..
gi 755545647 359 CLLICAEMYQVSRLQHICELFIITQLQ 385
Cdd:cd18339   94 VLLPAASLLQLMDVRQNCCDFLQSQLH 120