Domain of unknown function (DUF4734); This domain family is found in species of Drosophila, and is approximately 90 amino acids in length. The family is found in association with pfam07707.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875   336 RIVAQPIVRQAIHEGIAYTTTRMFYGKDREaFKHYLHKACVKPPVQRTWIYDRKCPYHHRMQCRNTVDLTYDAFLEYLNY 415
Cdd:pfam15881   1 EILQLPEVQALINEGLSYSTALMFEDKDPG-FRPLLEIFKVELPQQRRWIYDDGCPYHHDIKCPNTRYLTYEEFKSYLAR 79

                          90
                  ....*....|..
gi 24651875   416 TQRQHRDYWKSL 427
Cdd:pfam15881  80 LQTQGPDYWDTL 91

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 24651875    131 ITIGKTSHPVHLMVLQSFSRMFRDM---GNDLSVALPEKM--ITPRSFGLIYEWMIEDTPVLPRLGLLEVFHAAKFMEIP 205
Cdd:smart00225   4 LVVGGKKFHAHKAVLAAHSPYFKALfssDFKESDKSEIYLddVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIP 83

                           90
                   ....*....|..
gi 24651875    206 QLVRQCKYCLDH 217
Cdd:smart00225  84 GLVELCEEFLLK 95

Domain of unknown function (DUF4734); This domain family is found in species of Drosophila, and is approximately 90 amino acids in length. The family is found in association with pfam07707.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875   336 RIVAQPIVRQAIHEGIAYTTTRMFYGKDREaFKHYLHKACVKPPVQRTWIYDRKCPYHHRMQCRNTVDLTYDAFLEYLNY 415
Cdd:pfam15881   1 EILQLPEVQALINEGLSYSTALMFEDKDPG-FRPLLEIFKVELPQQRRWIYDDGCPYHHDIKCPNTRYLTYEEFKSYLAR 79

                          90
                  ....*....|..
gi 24651875   416 TQRQHRDYWKSL 427
Cdd:pfam15881  80 LQTQGPDYWDTL 91

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875    226 MLYFeAKILKLEVIHLQYLERVSKFFLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVT 305
Cdd:smart00875   4 IRRF-ADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSDDLNVSSEEEVFEAVLRWVKHDPEKRREHLP 82

                           90
                   ....*....|....*...
gi 24651875    306 DVVSSIRFGLIPPWLLIR 323
Cdd:smart00875  83 ELLEHVRLPLLSPDYLLE 100

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 24651875    131 ITIGKTSHPVHLMVLQSFSRMFRDM---GNDLSVALPEKM--ITPRSFGLIYEWMIEDTPVLPRLGLLEVFHAAKFMEIP 205
Cdd:smart00225   4 LVVGGKKFHAHKAVLAAHSPYFKALfssDFKESDKSEIYLddVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIP 83

                           90
                   ....*....|..
gi 24651875    206 QLVRQCKYCLDH 217
Cdd:smart00225  84 GLVELCEEFLLK 95

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 24651875 134 GKTSHPVHLMVLQSFSRMFRDMGNDLSVALPEKMITPRSFGLIYEWMIEDTPVLPRLGLLEVFHAAKFMEIPQLVRQCKY 213
Cdd:cd18299  21 GGVRIFAHRIVLAAASSVFADLFLMMTVVTLDSDITPEAFRRVLEFLYTGVLDENEDDLKELKDAAELLELFDLVMMCTN 100

                ..
gi 24651875 214 CL 215
Cdd:cd18299 101 VL 102

Domain of unknown function (DUF4734); This domain family is found in species of Drosophila, and is approximately 90 amino acids in length. The family is found in association with pfam07707.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875   336 RIVAQPIVRQAIHEGIAYTTTRMFYGKDREaFKHYLHKACVKPPVQRTWIYDRKCPYHHRMQCRNTVDLTYDAFLEYLNY 415
Cdd:pfam15881   1 EILQLPEVQALINEGLSYSTALMFEDKDPG-FRPLLEIFKVELPQQRRWIYDDGCPYHHDIKCPNTRYLTYEEFKSYLAR 79

                          90
                  ....*....|..
gi 24651875   416 TQRQHRDYWKSL 427
Cdd:pfam15881  80 LQTQGPDYWDTL 91

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875    226 MLYFeAKILKLEVIHLQYLERVSKFFLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVT 305
Cdd:smart00875   4 IRRF-ADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSDDLNVSSEEEVFEAVLRWVKHDPEKRREHLP 82

                           90
                   ....*....|....*...
gi 24651875    306 DVVSSIRFGLIPPWLLIR 323
Cdd:smart00875  83 ELLEHVRLPLLSPDYLLE 100

BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL2 and KLHL3; This subfamily includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. Both KLHL2 and KLHL3 function as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIPPWLLI 322
Cdd:cd18445  33 FSEVVKGEEFLLLSKEQVCELISSDDLTVPSEEKVFEAVMSWVNHDPENRKEHLAELLEHVRLPLLSPEYLV 104

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a BTB-Kelch protein that constitutes a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 cause autosomal-dominant retinitis pigmentosa.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24651875 247 VSKFFLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGL 315
Cdd:cd18447  30 IHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPYMVDILAKVRFPL 98

BACK (BTB and C-terminal Kelch) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also termed Kelch-like protein 27 (KLHL27), is an actin-binding protein that may play a role in organizing the actin cytoskeleton.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIPP 318
Cdd:cd18466  33 FLEVQSGEEFLGLTKDQLVKILRSEELSIEDEYQVFTAAMEWILKDVGKRKKHVVEVLEPVRFPLLPP 100

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 1 (KLHL1); KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. It may play a role in organizing the actin cytoskeleton in brain cells. KLHL1 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875 236 LEVIHLQYLERVskffLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGL 315
Cdd:cd18509  23 MKVAHSYTMENI----MEVIRNQEFLLLPAEELHKLLASDDVNVPDEETIFHALMMWVKYDMQRRCSDLSMLLAYIRLPL 98

                ....*.
gi 24651875 316 IPPWLL 321
Cdd:cd18509  99 LPPQLL 104

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 16 (KLHL16); Gigaxonin, also termed 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, such as tubulin folding cofactor B (TBCB), microtubule-associated protein MAP1B and glial fibrillary acidic protein (GFAP). Gigaxonin is mutated in giant axonal neuropathy.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24651875 242 QYLErvsKFFLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRF 313
Cdd:cd18455  26 EYLE---THFRDVSSTEEFLELSPEKLKELLSRDKLNVGNEEYIFEAVLRWVRHDPEERKVHLKDLMSSCWR 94

BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL25 and KLHL37; The family includes KLHL25 and KLHL37. 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 required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1). KLHL37, also called ectoderm-neural cortex protein 1 (ENC-1), or nuclear matrix protein NRP/B, or p53-induced gene 10 protein, is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIP 317
Cdd:cd18464  32 FTTLRKTEDFLSLPKDKLLELVSSEELEVEDERLVYEAVIGWIRYDLPRRHEVLPELLRSVRLALLP 98

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 2 (KLHL2); KLHL2, also called actin-binding protein Mayven, is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIPPWLLIR 323
Cdd:cd18512  33 FSDVVLSEEFLNLGIEQVCSLIASDKLTISSEEKVFEAVIAWVNHDKEVRQEHMAHLMEHVRLPLLSREYLVQ 105

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 40 (KLHL40); KLHL40, also called Kelch repeat and BTB domain-containing protein 5, or sarcosynapsin, 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. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIP 317
Cdd:cd18516  33 FQLIARDEDFLQLSPDELIAIISSDSLNVEKEEDVFEAVMKWVGKDQEERTKALPVLLESIRFRLMP 99

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 41 (KLHL41); KLHL41, also called Kel-like protein 23, or Kelch repeat and BTB domain-containing protein 10, or Kelch-related protein 1 (Krp1), or sarcosine, is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24651875 245 ERVSKFFLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIP 317
Cdd:cd18517  27 DFVSDRFEQISKEEDFLQLAPHELIAIISSDSLNVEKEELVFEAVMKWVRTDKENRVKSLGEIFDCIRFRLMP 99

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 24651875    131 ITIGKTSHPVHLMVLQSFSRMFRDM---GNDLSVALPEKM--ITPRSFGLIYEWMIEDTPVLPRLGLLEVFHAAKFMEIP 205
Cdd:smart00225   4 LVVGGKKFHAHKAVLAAHSPYFKALfssDFKESDKSEIYLddVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIP 83

                           90
                   ....*....|..
gi 24651875    206 QLVRQCKYCLDH 217
Cdd:smart00225  84 GLVELCEEFLLK 95

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 24651875   139 PVHLMVLQSFSRMFRDM-----GNDLSVALPEKMITPRSFGLIYEWMIEDTpVLPRLGLLEVFHAAKFMEIPQLVRQCKY 213
Cdd:pfam00651  23 RAHKAVLAACSPYFKALfsgqeSESSVSEITLDDVSPEDFEALLEFMYTGK-LISEENVDDLLAAADKLQIPSLVDKCEE 101

                  ....
gi 24651875   214 CLDH 217
Cdd:pfam00651 102 FLIK 105

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 34 (KLHL34); KLHL34 belongs to the KLHL family. Its function remains unclear. The methylation status of KLHL34 cg14232291 may be a predictive candidate of sensitivity to preoperative chemoradiation therapy.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875 259 EFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHwPQREENVTDVVSSIRFGLIPP 318
Cdd:cd18473  45 GLLELNLESLQAVLEADDIPRVKESRLLTLVLEWLNQD-ESRLAYANALLSRIRYGLVPV 103

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 36 (KLHL36); KLHL36 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875 237 EVIHLQYLERVSKF--------FLTLVASKEFLR-LPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHwPQREENVTDV 307
Cdd:cd18475  11 ELASIYSLERLDSFidsfilqnFGTLSFTPDFLQnVSMQKLCQYLSSNQVQHECEHDLLQAALQWLTQS-PERENEAYQV 89

                        90
                ....*....|
gi 24651875 308 VSSIRFGLIP 317
Cdd:cd18475  90 LSNIHFPLIP 99

BACK (BTB and C-terminal Kelch) 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 required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1).

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIP 317
Cdd:cd18514  33 FETVRESEDFYSLSKDKLLDLISSDELEIEDEQVVFNAVLQWVKYDLEKRKDYLPELLRNVRLALLP 99

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 3 (ZBTB3); ZBTB3 is a transcription factor essential for cancer cell growth via the regulation of the reactive oxygen species (ROS) detoxification pathway. ZBTB3 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875 119 SLVKQRTK---TNSEITIGKTSHPVHLMVLQSFSRMF------RDMGNDLsVALPEKMITPRSFGLIYEWMIE------D 183
Cdd:cd18323  13 SLREQRHQgflCDCTVLVGSTQFLAHRAVLASCSPFFhmfykeQLDKRDL-VCINNEIVTAPAFSLLLEFMYEgrlsfnD 91

                        90       100
                ....*....|....*....|....*....
gi 24651875 184 TPVlprlglLEVFHAAKFMEIPQLVRQCK 212
Cdd:cd18323  92 TPV------EDVLAAASYLHMNDIVKVCK 114

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 37 (KLHL37); KLHL37, also called ectoderm-neural cortex protein 1 (ENC-1), or nuclear matrix protein NRP/B, or p53-induced gene 10 protein, is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24651875 251 FLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSHHWPQREENVTDVVSSIRFGLIP 317
Cdd:cd18515  32 FQTICKTEDFLQLPKDMVVQLLSSEELETEDERLVYEAAINWVNYDLKKRHCYLSELLQTVRLALLP 98

BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 3 (KBTBD3); KBTBD3, also termed BTB and kelch domain-containing protein 3 (BKLHD3), is a BTB-Kelch family protein. Its function remains unclear.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24651875 244 LERVSKFFLTLVASKEFLRLPLKSMLLLIQSDLIGVNTELEVFMAAARWLSH 295
Cdd:cd18480  26 LEFVMQHFSLLSQSQEFLELNFEVLEKILEADELNVPDEEAVLKAVLRWTKH 77

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 40 (ZBTB40); ZBTB40 may be involved in transcriptional regulation. Single-nucleotide polymorphisms of ZBTB40 are associated with bone mineral density in European and East-Asian populations. ZBTB40 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875 113 LYQQIVSLVKQRTKTNSEITIGKTSHPVHLMVLQSFSRMFRDM--GNDlSVALPEKMITPRSFGLIYEWM 180
Cdd:cd18225  10 LLQQLHTLRKEQQFCDCTIFIGTFHFRAHKLVLAASSLLFKSLldSTD-TISIDASVVSPEEFALLLEMV 78

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24651875 130 EITIGKTSHPVHLMVLQSFSRMFRDM-------GNDLSVALPEkmITPRSFGLIYEWMIEDTPVLPRLGLLEVFHAAKF 201
Cdd:cd18186   5 TLVVGGREFPAHRAVLAARSPYFRAMfssgmkeSSSSEIELDD--VSPEAFEALLDYIYTGELELSEENVEELLAAADK 81

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing proteins, ZBTB3, ZBTB18, ZBTB42 and similar proteins; The family includes zinc finger and BTB domain-containing proteins, ZBTB3, ZBTB18 and ZBTB42. ZBTB3 is a transcription factor essential for cancer cell growth via the regulation of the reactive oxygen species (ROS) detoxification pathway. ZBTB18 is a sequence-specific transrepressor associated with heterochromatin. ZBTB42 is a transcriptional repressor that specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. Members of this family contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651875 115 QQIVSLVKQRTK---TNSEITIGKTSHPVHLMVLQSFSRMF------RDMGNDLsVALPEKMITPRSFGLIYEWMIEDTP 185
Cdd:cd18194   9 QLLQCLREQRSQgflCDCTVLVGSAQFPAHRAVLASCSMYFhlfyrdRLDKRDL-VRLNSDIVTAPAFGLLLDFMYEGRL 87

                        90       100
                ....*....|....*....|....*..
gi 24651875 186 VLPRLGLLEVFHAAKFMEIPQLVRQCK 212
Cdd:cd18194  88 ALRDLPVEDVLAAASYLHMYDIVKVCK 114