BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with various functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). It contains an ankyrin repeat, BTB/POZ, and BACK domains. 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 300796366  820 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSKTIEISDIKYHIFQM 899
Cdd:cd18350     1 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEISDIKYHIFQM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796366  900 LMQYLYYGGTESMEIPTADILQLLSAANLFQLDALQRHCEILCSQTLSVESAVN 953
Cdd:cd18350    81 LMQYLYYGGTESMEIPIADVLELLSAASLFQLDALQRHCEILCSQTINLENAVN 134

BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications in Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300796366  946 LSVESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQSTLAERVHSVYVTSRV 1024
Cdd:cd18526     1 INLENSVSIYKYAKIHNAPELASFCEGFFLKNMKALLEQDSFRQLIYGRNSKVQGLDPLQDLQVTLAKRMHSIYITSRV 79

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with various functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). It contains an ankyrin repeat, BTB/POZ, and BACK domains. 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 300796366  820 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSKTIEISDIKYHIFQM 899
Cdd:cd18350     1 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEISDIKYHIFQM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796366  900 LMQYLYYGGTESMEIPTADILQLLSAANLFQLDALQRHCEILCSQTLSVESAVN 953
Cdd:cd18350    81 LMQYLYYGGTESMEIPIADVLELLSAASLFQLDALQRHCEILCSQTINLENAVN 134

BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications in Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300796366  946 LSVESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQSTLAERVHSVYVTSRV 1024
Cdd:cd18526     1 INLENSVSIYKYAKIHNAPELASFCEGFFLKNMKALLEQDSFRQLIYGRNSKVQGLDPLQDLQVTLAKRMHSIYITSRV 79

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 300796366   836 HFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgDNSKTIEISDIKYHIFQMLMQYLYYGGTesmeIP 915
Cdd:pfam00651    3 ELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESE--SSVSEITLDDVSPEDFEALLEFMYTGKL----IS 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 300796366   916 TADILQLLSAANLFQLDALQRHCEILCSQTL 946
Cdd:pfam00651   77 EENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107

Ankyrin repeats (3 copies);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366   526 LMYACATGDEAMVQMLIDAGANLDIQvpsnsprhpsvhpDSRHWTSLTFAVLHGHISVVQLLLDagaHVEGSAVNSGEds 605
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-------------DKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGR-- 62

                           90       100
                   ....*....|....*....|....*...
gi 300796366   606 yaeTPLQLASAAGNYELVSLLLSRGADP 633
Cdd:pfam12796   63 ---TALHYAARSGHLEIVKLLLEKGADI 87

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366  521 QGLTPLMYACATGDEAMVQMLIDAGANLDIqvpsnsprhpsvhPDSRHWTSLTFAVLHGHISVVQLLLDAgahvegSAVN 600
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDI-------------PNTDKFSPLHLAVMMGDIKGIELLIDH------KACL 161

                          90       100       110
                  ....*....|....*....|....*....|...
gi 300796366  601 SGEDSYAETPLQLASAAGNYELVSLLLSRGADP 633
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

Histone H2A [Chromatin structure and dynamics];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 300796366  198 SARCGLTFSVGRFFRWMVDTRISVRIHEYAAISLTACMENLVEEI 242
Cdd:COG5262    20 SAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEI 64

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300796366  570 TSLTFAVLHGHISVVQLLLDAGAHVE-----GSAVNSGEDS---YAETPLQLASAAGNYELVSLLLSRGADP 633
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratGTFFRPGPKNliyYGEHPLSFAACVGNEEIVRLLIEHGADI 162

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with various functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). It contains an ankyrin repeat, BTB/POZ, and BACK domains. 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 300796366  820 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSKTIEISDIKYHIFQM 899
Cdd:cd18350     1 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEISDIKYHIFQM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796366  900 LMQYLYYGGTESMEIPTADILQLLSAANLFQLDALQRHCEILCSQTLSVESAVN 953
Cdd:cd18350    81 LMQYLYYGGTESMEIPIADVLELLSAASLFQLDALQRHCEILCSQTINLENAVN 134

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 11 (BTBD11); BTBD11, also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11, is a BTB-domain-containing protein. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. 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 300796366  820 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGdnsKTIEISDIKYHIFQM 899
Cdd:cd18351     1 PKLTEIKRKQTSRLDPHFLNNKEMSDVTFLVEGRPFYAHKVLLFTASPRFKALLSNKPSAEN---TCIEISYVKYHIFQL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796366  900 LMQYLYYGGTESMEIPTADILQLLSAANLFQLDALQRHCEILCSQTLSVESAVN 953
Cdd:cd18351    78 VMQYLYCGGTESLLIKNNEIMELLSAAKFFQLEALQRHCEIICAKSINTENCVD 131

BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications in Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300796366  946 LSVESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQSTLAERVHSVYVTSRV 1024
Cdd:cd18526     1 INLENSVSIYKYAKIHNAPELASFCEGFFLKNMKALLEQDSFRQLIYGRNSKVQGLDPLQDLQVTLAKRMHSIYITSRV 79

BACK (BTB and C-terminal Kelch) domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins involved in a range of functions from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications in Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN). This subfamily also includes BTB/POZ domain-containing protein 11 (BTBD11), whose function is unclear.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300796366  946 LSVESAVNTYKYAKIHNAPELALFCEGFFLKHMK-ALLEQDAFRQLIYGrsSKVQGLDPLQDLQSTLAERVHSV 1018
Cdd:cd18491     1 LDLDNVVAIYKHAKLYNAPELLAYCEGYFLQNMVqLLLENDSFRKLLFG--KKLHGHDVLQGLQATLTQRIQSR 72

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366  487 NQDLGFRMLNCGRTDLISQAIEALGPDGVNTMDDQGLTPLMYACATGDEAMVQMLIDAGANLDIQvpsnsprhpsvhpDS 566
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-------------DK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366  567 RHWTSLTFAVLHGHISVVQLLLDAGAHVEGSavnsgeDSYAETPLQLASAAGNYELVSLLLSRGADPllsMLEANGMASS 646
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQ------DNDGNTPLHLAAANGNLEIVKLLLEAGADV---NARDNDGETP 189

                         170       180       190
                  ....*....|....*....|....*....|....
gi 300796366  647 LHedmncfsHSAAHGHRNVLRKLLtqpqQAKADV 680
Cdd:COG0666   190 LH-------LAAENGHLEIVKLLL----EAGADV 212

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 300796366  833 LDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgDNSKTIEISDIKYHIFQMLMQYLYYGgteSM 912
Cdd:cd18352     3 LGEQYVNNATLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYRE--KEARDIEIPNIRWEVFELMMRFIYTG---SV 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 300796366  913 EIpTADILQ-LLSAANLFQLDALQRHCEILCSQTLSVES 950
Cdd:cd18352    78 DI-TNDIAKdLLRAADQYLLEGLKRLCEYTIAQDLTLEN 115

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 300796366    845 DVTFLVEGKLFYAHKVLLVTASNRFKTLMTNksEQDGDNSKTIEISDIKYHIFQMLMQYLYyggTESMEIPTADILQLLS 924
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSS--DFKESDKSEIYLDDVSPEDFRALLNFLY---TGKLDLPEENVEELLE 75

                            90       100
                    ....*....|....*....|..
gi 300796366    925 AANLFQLDALQRHCEILCSQTL 946
Cdd:smart00225   76 LADYLQIPGLVELCEEFLLKLL 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 300796366  838 LNNKEMSDVTFLV--EGKLFYAHKVLLVTASNRFKTlMTNKSEQDGDNSKTIEISDIKYHIFQMLMQYLYyggTESMEIP 915
Cdd:cd18294     9 INNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRA-MFLTGPQKESTQSPLVLSDIEPEVFRAVLEFIY---TNCVTLS 84

                          90       100
                  ....*....|....*....|....
gi 300796366  916 TADILQLLSAANLFQLDALQRHCE 939
Cdd:cd18294    85 NHTVIEVLAAAVEYGLDELRKLCE 108

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366  836 HFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTN---KSEqdgdnSKTIEISDIKYHIFQMLMQYLYyggTESM 912
Cdd:cd18300     2 LFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGnfrESS-----AKEVELPGVSKETFLALLEYLY---TDQA 73

                          90       100
                  ....*....|....*....|....*...
gi 300796366  913 -EIPTADILQLLSAANLFQLDALQRHCE 939
Cdd:cd18300    74 pILEDGDCVGLIVLANRLCLPRLVALCE 101

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in plant BTB/POZ-MATH (BPM) protein family; The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins from other plants. BPM protein, also called protein BTB-POZ and MATH domain, may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366  838 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEqdGDNSKTIEISDIKYHIFQMLMQYLYY---------GG 908
Cdd:cd18280     9 LESEEGADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMR--EENEGEIVIEDVEPPVFKALLHFIYKdelpddvepAG 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 300796366  909 TESMEIPTADILQLLSAANLFQLDALQRHCE-ILC 942
Cdd:cd18280    87 SDSSSLDTTMAQHLLAAADRYALERLRLLCEsRLC 121

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 300796366  823 PEIRKTLPARLDPHFlNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgdnskTIEISDIKYHIFQMLMQ 902
Cdd:cd18354     1 PDDHLTVAESLKREF-DNPDTADLKFLVDGKYIYVHKVLLKIRCEHFRSLLNENEEE------IIEMSQFSYPVYRAFLE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300796366  903 YLYyggTESMEIPTADILQLLSAANLFQLDALQRhceiLCSQTL 946
Cdd:cd18354    74 YLY---TDSISLSPEDAIGLLDLATFYRENRLKK----LCQQTI 110

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 17 (BTBD17); BTBD17, also called galectin-3-binding protein-like, is a BTB domain-containing protein. Its function remains unclear. It may be associated with 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 300796366  837 FLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSKtIEI--SDIKYHIFQMLMQYLYYGgteSMEI 914
Cdd:cd18292    11 LYNNEELSDIVLRVGGKVFHAHRLILAKSSDVFRVMLSNDWWSESKQSE-IELveDPECAAVFEKFLRYLYTG---QISV 86

                          90       100
                  ....*....|....*....|....*
gi 300796366  915 PTADILQLLSAANLFQLDALQRHCE 939
Cdd:cd18292    87 NLETALPLLMLADKYNVTDLKQLCV 111

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins; Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796366  836 HFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSktIEISDIKYHIFQMLMQYLYYGGTESMEiP 915
Cdd:cd18345    11 LLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNR--VEITDVDHEVMREMLRFIYTGKAPNLD-K 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 300796366  916 TADilQLLSAANLFQLDALQRHC-EILCSqTLSVESA 951
Cdd:cd18345    88 MAD--DLLAAADKYALERLKVMCeEALCS-NLSVENV 121

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 300796366  838 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLmtnkseqDGDNSKTIEISDIKYHIFQMLMQYLYyggTESMEIPTA 917
Cdd:cd18303    13 FDKELYSDITIKLADKSIPAHKFVLAARSEKWSNE-------NLASTNELDLSDISYEVVLALLRWLY---TDELDLTLD 82

                          90       100
                  ....*....|....*....|....
gi 300796366  918 DI--LQLLSAANLFQLDALQRHCE 939
Cdd:cd18303    83 DEflLELMKAAKRFQLTDLVERCE 106

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 300796366  838 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSktIEISDIKYHIFQMLMQYLYYGGTESMEIPTA 917
Cdd:cd18279    13 WENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNR--VEINDVDPEVFKEMMRFIYTGKAPNLDKMAD 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 300796366  918 DilqLLSAANLFQLDALQRHCE-ILCSqTLSVES 950
Cdd:cd18279    91 D---LLAAADKYALERLKVMCEdALCS-NLSVEN 120

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 300796366  838 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgDNSKTIEISDIKYHIFQMLMQYLYYGgteSMEIPTA 917
Cdd:cd18314     1 YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIE--SNLKEVTLEDVEPEIFETVLKYMYTG---QVTLSEE 75

                          90       100
                  ....*....|....*....|.
gi 300796366  918 DILQLLSAANLFQLDALQRHC 938
Cdd:cd18314    76 NVLDLLMLASKYQVPDLEKLC 96

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 12 (KLHL12); KLHL12, also called CUL3-interacting protein 1 (C3IP1) or DKIR homolog, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of the Wnt signaling pathway and ER-Golgi transport. 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 300796366  845 DVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDNSktIEISDIKYHIFQMLMQYLYyggTESMEIPTADILQLLS 924
Cdd:cd18242    23 DVTLRVEGKEFPAHRIVLAACSDYFCAMFTSEMSEKGKSE--VELQGLTASTMEILLDFVY---TETVHVTVENVQELLP 97

                          90       100
                  ....*....|....*....|.
gi 300796366  925 AANLFQLDALQRHC-EILCSQ 944
Cdd:cd18242    98 AACLLQLKGVKQACcEFLESQ 118

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 29 (KLHL29); KLHL29 is also called Kelch repeat and BTB domain-containing protein 9 (KBTBD9). A novel fusion transcript NR5A2-KLHL29FT, resulting from transchromosomal insertion, may influence the origin or progression of colon cancer. KLHL29 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 300796366  841 KEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMtNKSEQDGDNSKTIEI--SDIKYHIFQMLMQYLYYGgteSMEIPTAD 918
Cdd:cd18258    15 KEFTDLKIIVEGKEFEVHQNVLASCSLYFKDLI-KRSSRDSGGGEKLELtmSNINADVLELLLEFVYTG---SLIIDSAN 90

                          90       100
                  ....*....|....*....|
gi 300796366  919 ILQLLSAANLFQLDALQRHC 938
Cdd:cd18258    91 AKTLLEAANKFQFHTFCKVC 110

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4); KBTBD4, also called BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates. 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 300796366  838 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDnsKTIEISDIKYHIFQMLMQYLYYGgteSMEIPTA 917
Cdd:cd18272    27 LEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARN--RVIELKDVSESVFQLLVDYIYHG---TVKLRVE 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 300796366  918 DILQLLSAANLFQLDALQRHCEILCSQTLSV 948
Cdd:cd18272   102 ELQETYEVADMYQLTALFEECSRFLARTVQV 132

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 300796366  842 EMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMT---NKSEQDgdnskTIEISDIKYHIFQMLMQYLYYGgteSMEIPTAD 918
Cdd:cd18256    19 EFCDVQLQVGMELFSVHRLVLAASSPYFAALFAggmSESSKD-----VVQIHGVEPDIFHILLDFIYTG---VVEVTVSN 90

                          90       100
                  ....*....|....*....|....*...
gi 300796366  919 ILQLLSAANLFQL-DALQRHCEILCSQT 945
Cdd:cd18256    91 VQELLVAADMLQLtEVVEICCEFLKGQL 118