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 300796386  821 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDSSKTIEISDMKYHIFQM 900
Cdd:cd18350     1 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEISDIKYHIFQM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796386  901 MMQYLYYGGTESMEIPTTDILELLSAASLFQLDALQRHCEILCSQTLSMESAVN 954
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 300796386  947 LSMESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQNTLAERVHSVYITSRV 1025
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 300796386  821 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDSSKTIEISDMKYHIFQM 900
Cdd:cd18350     1 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEISDIKYHIFQM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796386  901 MMQYLYYGGTESMEIPTTDILELLSAASLFQLDALQRHCEILCSQTLSMESAVN 954
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 300796386  947 LSMESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQNTLAERVHSVYITSRV 1025
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 300796386   837 HFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgDSSKTIEISDMKYHIFQMMMQYLYYGGTesmeIP 916
Cdd:pfam00651    3 ELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESE--SSVSEITLDDVSPEDFEALLEFMYTGKL----IS 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 300796386   917 TTDILELLSAASLFQLDALQRHCEILCSQTL 947
Cdd:pfam00651   77 EENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107

Ankyrin repeats (3 copies);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386   526 LMYACAAGDEAMVQMLIDAGANLDIQvpsnsprhpsihpDSRHWTSLTFAVLHGHISVVQLLLDAgahvegsaVNGGEDS 605
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-------------DKNGRTALHLAAKNGHLEIVKLLLEH--------ADVNLKD 59

                           90       100
                   ....*....|....*....|....*...
gi 300796386   606 YAETPLQLASAAGNYELVSLLLSRGADP 633
Cdd:pfam12796   60 NGRTALHYAARSGHLEIVKLLLEKGADI 87

kelch-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  843 EMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSeqdgdSSKTIEISDmKYHIFQMMMQYLYyggTESMEIPTTDILE 922
Cdd:PHA03098   10 CDESIIIVNGGGIIKVHKIILSSSSEYFKKMFKNNF-----KENEINLNI-DYDSFNEVIKYIY---TGKINITSNNVKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 300796386  923 LLSAASLFQLDALQRHCEILCSQTLSMESAVNTYKYAKIHN 963
Cdd:PHA03098   81 ILSIANYLIIDFLINLCINYIIKIIDDNNCIDIYRFSFFYG 121

Histone H2A [Chromatin structure and dynamics];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  198 SARCGLTFSVGRFFRWMVDTRISVRIHEYAAISLTACMENLVEEI------------RARVMASHspdgggagggevsae 265
Cdd:COG5262    20 SAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEIlelagnaardnkKKRIIPRH--------------- 84

                          90
                  ....*....|..
gi 300796386  266 aLEMVINNDAEL 277
Cdd:COG5262    85 -LQLAIRNDEEL 95

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 300796386  570 TSLTFAVLHGHISVVQLLLDAGAHVEGSAVNG-----GEDS---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 300796386  821 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDSSKTIEISDMKYHIFQM 900
Cdd:cd18350     1 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKSLLTNKSEQESQGSKTIEISDIKYHIFQM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796386  901 MMQYLYYGGTESMEIPTTDILELLSAASLFQLDALQRHCEILCSQTLSMESAVN 954
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 300796386  821 PSIPEIRKTLPARLDPHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGdssKTIEISDMKYHIFQM 900
Cdd:cd18351     1 PKLTEIKRKQTSRLDPHFLNNKEMSDVTFLVEGRPFYAHKVLLFTASPRFKALLSNKPSAEN---TCIEISYVKYHIFQL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300796386  901 MMQYLYYGGTESMEIPTTDILELLSAASLFQLDALQRHCEILCSQTLSMESAVN 954
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 300796386  947 LSMESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQNTLAERVHSVYITSRV 1025
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 300796386  947 LSMESAVNTYKYAKIHNAPELALFCEGFFLKHMK-ALLEQDAFRQLIYGrsSKVQGLDPLQDLQNTLAERVHSV 1019
Cdd:cd18491     1 LDLDNVVAIYKHAKLYNAPELLAYCEGYFLQNMVqLLLENDSFRKLLFG--KKLHGHDVLQGLQATLTQRIQSR 72

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  477 LDARAATEKFNQDLGFRMLNCGRTDLINQAIEALGPDGVNTMDDQGMTPLMYACAAGDEAMVQMLIDAGANLDIQvpsns 556
Cdd:COG0666    42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR----- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  557 prhpsihpDSRHWTSLTFAVLHGHISVVQLLLDAGAHVEGSavnggeDSYAETPLQLASAAGNYELVSLLLSRGADPlls 636
Cdd:COG0666   117 --------DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ------DNDGNTPLHLAAANGNLEIVKLLLEAGADV--- 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300796386  637 MLEAHGMGSSLHedmncfsHSAAHGHRNVLRKLLtqpqQAKADV 680
Cdd:COG0666   180 NARDNDGETPLH-------LAAENGHLEIVKLLL----EAGADV 212

BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 11 (BTBD11); BTBD11, also termed ankyrin repeat and BTB/POZ domain-containing protein BTBD11, is a BTB-domain-containing Kelch-like protein. Its function remains unclear. The BTBD11 gene has been identified as an all-trans retinoic acid-responsive gene that may play a role in neural development.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300796386  947 LSMESAVNTYKYAKIHNAPELALFCEGFFLKHMKALLEQDAFRQLIYGRSSKVQGLDPLQDLQNTLAERVHSVYITS 1023
Cdd:cd18527     1 INTENCVDIYNHAKFLGATELSSYCEGYFLKNMVLLIENEAFKQLLYDKNGESPGQDVLQDLERTLATRIQSIHLSS 77

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 300796386    846 DVTFLVEGKLFYAHKVLLVTASNRFKTLMTNksEQDGDSSKTIEISDMKYHIFQMMMQYLYyggTESMEIPTTDILELLS 925
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSS--DFKESDKSEIYLDDVSPEDFRALLNFLY---TGKLDLPEENVEELLE 75

                            90       100
                    ....*....|....*....|..
gi 300796386    926 AASLFQLDALQRHCEILCSQTL 947
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 300796386  839 LNNKEMSDVTFLV--EGKLFYAHKVLLVTASNRFKTlMTNKSEQDGDSSKTIEISDMKYHIFQMMMQYLYyggTESMEIP 916
Cdd:cd18294     9 INNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRA-MFLTGPQKESTQSPLVLSDIEPEVFRAVLEFIY---TNCVTLS 84

                          90       100
                  ....*....|....*....|....
gi 300796386  917 TTDILELLSAASLFQLDALQRHCE 940
Cdd:cd18294    85 NHTVIEVLAAAVEYGLDELRKLCE 108

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 300796386  840 NNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMtnKSEQDGDSSKTIEISDMKYHIFQMMMQYLYyggTESMEIPTTD 919
Cdd:cd18298     8 NDPRTSDLKFRVDGKYIYVHKAILKIRCEYFRSMF--QSHWNEDDKNVIEIDQYSYPVYYAFLRYLY---TDQVDLPPED 82

                          90       100
                  ....*....|....*....|.
gi 300796386  920 ILELLSAASLFQLDALQRHCE 940
Cdd:cd18298    83 AIGLLDLANSYCEERLKKLCE 103

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 300796386  837 HFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTnkseqdGD----SSKTIEISDMKYHIFQMMMQYLYyggTES 912
Cdd:cd18300     2 LFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFG------GNfresSAKEVELPGVSKETFLALLEYLY---TDQ 72

                          90       100
                  ....*....|....*....|....*....
gi 300796386  913 M-EIPTTDILELLSAASLFQLDALQRHCE 940
Cdd:cd18300    73 ApILEDGDCVGLIVLANRLCLPRLVALCE 101

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 300796386  824 PEIRKTLPARLDPHFlNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgdsskTIEISDMKYHIFQMMMQ 903
Cdd:cd18354     1 PDDHLTVAESLKREF-DNPDTADLKFLVDGKYIYVHKVLLKIRCEHFRSLLNENEEE------IIEMSQFSYPVYRAFLE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 300796386  904 YLYyggTESMEIPTTDILELLSAASLFQLDALQRHCEILCSQTLSME 950
Cdd:cd18354    74 YLY---TDSISLSPEDAIGLLDLATFYRENRLKKLCQQTIKQGICEE 117

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. 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 300796386  839 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLM------TNKSEqdgdssktIEISDMKYHIFQMMMQYLYYGGTES 912
Cdd:cd18287    17 FLNEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLyggmreSQQSE--------IELKDTNAEAFKALLKYIYTGRLTL 88

                          90       100
                  ....*....|....*....|....
gi 300796386  913 MEIPTTDILELLSAASLFQLDALQ 936
Cdd:cd18287    89 TDLKEDVLLDVLGLAHQYGFEELE 112

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 300796386  839 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLmtnkseqDGDSSKTIEISDMKYHIFQMMMQYLYyggTESMEIPTT 918
Cdd:cd18303    13 FDKELYSDITIKLADKSIPAHKFVLAARSEKWSNE-------NLASTNELDLSDISYEVVLALLRWLY---TDELDLTLD 82

                          90       100
                  ....*....|....*....|....
gi 300796386  919 DI--LELLSAASLFQLDALQRHCE 940
Cdd:cd18303    83 DEflLELMKAAKRFQLTDLVERCE 106

Ankyrin repeats (3 copies);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386   498 GRTDLINQAIEAlgPDGVNTMDDQGMTPLMYACAAGDEAMVQMLIDaganldiqvpsnsprHPSIHPDSRHWTSLTFAVL 577
Cdd:pfam12796    8 GNLELVKLLLEN--GADANLQDKNGRTALHLAAKNGHLEIVKLLLE---------------HADVNLKDNGRTALHYAAR 70

                           90
                   ....*....|....*..
gi 300796386   578 HGHISVVQLLLDAGAHV 594
Cdd:pfam12796   71 SGHLEIVKLLLEKGADI 87

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also called HIB homolog 2 or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes may contain homodimeric SPOPL or the heterodimers formed by speckle-type POZ protein (SPOP) and SPOPL, which are less efficient than ubiquitin ligase complexes containing only SPOP. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  837 HFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgdSSKT-IEISDMKYHIFQMMMQYLYYGGTESMEi 915
Cdd:cd18343    14 NLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEE---SKKNrVEINDVDPEVFKEMMRFIYTGKAPNLD- 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 300796386  916 PTTDilELLSAASLFQLDALQRHC-EILCSqTLSMES 951
Cdd:cd18343    90 KMAD--NLLAAADKYALERLKVMCeEALCN-NLSVEN 123

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 300796386  839 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQdgDSSKTIEISDMKYHIFQMMMQYLYYGgteSMEIPTT 918
Cdd:cd18314     1 YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIE--SNLKEVTLEDVEPEIFETVLKYMYTG---QVTLSEE 75

                          90       100
                  ....*....|....*....|.
gi 300796386  919 DILELLSAASLFQLDALQRHC 939
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 300796386  846 DVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDSSktIEISDMKYHIFQMMMQYLYyggTESMEIPTTDILELLS 925
Cdd:cd18242    23 DVTLRVEGKEFPAHRIVLAACSDYFCAMFTSEMSEKGKSE--VELQGLTASTMEILLDFVY---TETVHVTVENVQELLP 97

                          90       100
                  ....*....|....*....|.
gi 300796386  926 AASLFQLDALQRHC-EILCSQ 945
Cdd:cd18242    98 AACLLQLKGVKQACcEFLESQ 118

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 300796386  843 EMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTnkSEQDGDSSKTIEISDMKYHIFQMMMQYLYYGgteSMEIPTTDILE 922
Cdd:cd18256    19 EFCDVQLQVGMELFSVHRLVLAASSPYFAALFA--GGMSESSKDVVQIHGVEPDIFHILLDFIYTG---VVEVTVSNVQE 93

                          90       100
                  ....*....|....*....|....*
gi 300796386  923 LLSAASLFQL-DALQRHCEILCSQT 946
Cdd:cd18256    94 LLVAADMLQLtEVVEICCEFLKGQL 118

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 300796386  839 LNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDGDssKTIEISDMKYHIFQMMMQYLYYGgteSMEIPTT 918
Cdd:cd18272    27 LEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARN--RVIELKDVSESVFQLLVDYIYHG---TVKLRVE 101

                          90       100
                  ....*....|....*....|....*....
gi 300796386  919 DILELLSAASLFQLDALQRHCEILCSQTL 947
Cdd:cd18272   102 ELQETYEVADMYQLTALFEECSRFLARTV 130

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in TD and POZ domain-containing proteins (TDPOZ); TDPOZ is a family of bipartite animal and plant proteins that contains a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. This subfamily contains only mammalian members. Plant TDPOZ proteins contain a MATH domain at the N-terminal region and are named "BTB/POZ and MATH domain-containing proteins (BPM)", not included in this subfamily. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  821 PSIPEIRKTLPARLDpHFLNNKEMSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTNKSEQDgdSSKTIEISDMKYHIFQM 900
Cdd:cd18344     1 PAIKDPRHMLTDDLG-ELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEER--LKNPIEIHDLDPQVFKE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300796386  901 MMQYLYYGGTESMEIPTTdILELLSAASLFQLDALQRHCEILCSQTLSMESA 952
Cdd:cd18344    78 MMGFIYTGKAPHLHSHSM-ACDVLAAADKYGLEGLKVLCEDALCRNLSVENA 128

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796386  844 MSDVTFLVEGKLFYAHKVLLVTASNRFKTLMTN---KSEQDgdsskTIEISDMKYHIFQMMMQYLYYGgteSMEIPTTDI 920
Cdd:cd18247    19 LCDVTLKVGDQKFSAHRIVLAATIPYFHAMFTHdmvESKQD-----EITMQGIEPSALEALINFAYSG---RIAIDTSNV 90