second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. This model corresponds to the 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 115430108 410 LKFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIF 489
Cdd:cd18360    1 LGLFFNSPLLADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCPASIL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 115430108 490 QAMCLLICAEMYQVSRLQHICELFIITQLQ 519
Cdd:cd18360   81 QAMALLICAEMYQVSRLQHICELYIITQLQ 110

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108  34 LVSGDES---SLLLNAASTVARPvfTEYQASAFGN--VKLVVHDCPV----WDIFDSDWYTS-RNLI-GGADIIVIKYNV 102
Cdd:cd00157    4 VVVGDGAvgkTCLLISYTTNKFP--TEYVPTVFDNysANVTVDGKQVnlglWDTAGQEEYDRlRPLSyPQTDVFLLCFSV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115430108 103 NDKFSFHEVKDNYIPVIKRALNSVPVIIaaVGT----RQNEELPCTcplcTSDRGSCVSTTEGIQLAKELGAT-YLE 174
Cdd:cd00157   82 DSPSSFENVKTKWYPEIKHYCPNVPIIL--VGTkidlRDDGNTLKK----LEKKQKPITPEEGEKLAKEIGAVkYME 152

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. This model corresponds to the 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 115430108 410 LKFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIF 489
Cdd:cd18360    1 LGLFFNSPLLADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCPASIL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 115430108 490 QAMCLLICAEMYQVSRLQHICELFIITQLQ 519
Cdd:cd18360   81 QAMALLICAEMYQVSRLQHICELYIITQLQ 110

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 115430108  413 FLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGifQAM 492
Cdd:pfam00651   4 LREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEE--NVD 81

                          90       100
                  ....*....|....*....|....*.
gi 115430108  493 CLLICAEMYQVSRLQHICELFIITQL 518
Cdd:pfam00651  82 DLLAAADKLQIPSLVDKCEEFLIKSL 107

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108  34 LVSGDES---SLLLNAASTVARPvfTEYQASAFGN--VKLVVHDCPV----WDIFDSDWYTS-RNLI-GGADIIVIKYNV 102
Cdd:cd00157    4 VVVGDGAvgkTCLLISYTTNKFP--TEYVPTVFDNysANVTVDGKQVnlglWDTAGQEEYDRlRPLSyPQTDVFLLCFSV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115430108 103 NDKFSFHEVKDNYIPVIKRALNSVPVIIaaVGT----RQNEELPCTcplcTSDRGSCVSTTEGIQLAKELGAT-YLE 174
Cdd:cd00157   82 DSPSSFENVKTKWYPEIKHYCPNVPIIL--VGTkidlRDDGNTLKK----LEKKQKPITPEEGEKLAKEIGAVkYME 152

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108    92 GADIIVIKYNVNDKFSFHEVKDNYIPVIKRALNSVPVIIaaVGTR--QNEELPCTCPLCTsDRGSCVSTTEGIQLAKELG 169
Cdd:smart00174  69 DTDVFLICFSVDSPASFENVKEKWYPEVKHFCPNVPIIL--VGTKldLRNDKSTLEELSK-KKQEPVTYEQGQALAKRIG 145

                   ....*.
gi 115430108   170 A-TYLE 174
Cdd:smart00174 146 AvKYLE 151

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. This model corresponds to the 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 115430108 410 LKFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIF 489
Cdd:cd18360    1 LGLFFNSPLLADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCPASIL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 115430108 490 QAMCLLICAEMYQVSRLQHICELFIITQLQ 519
Cdd:cd18360   81 QAMALLICAEMYQVSRLQHICELYIITQLQ 110

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 115430108 411 KFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIFQ 490
Cdd:cd18300    1 KLFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGNFRESSAKEVELPGVSKETFLALLEYLYTDQAPILEDGD 80

                         90       100
                 ....*....|....*....|....*...
gi 115430108 491 AMCLLICAEMYQVSRLQHICELFIITQL 518
Cdd:cd18300   81 CVGLIVLANRLCLPRLVALCEQYIVKEL 108

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 115430108 242 SDLNNLLFCCQCVDVVFYNPnLKKVVEAHKIVLCAVSHVFMLLFNVksptdiqdssiirttqdlfainrdtafpgashes 321
Cdd:cd18299    1 EDLRNLLHSPSCADVVFILQ-GGVRIFAHRIVLAAASSVFADLFLM---------------------------------- 45

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115430108 322 sgnppLRVIVKDALF-CSCLSDILRFIYSGAFQWeelEEDIRKKLKDSGDVSNVIEkVKCILKTPGK 387
Cdd:cd18299   46 -----MTVVTLDSDItPEAFRRVLEFLYTGVLDE---NEDDLKELKDAAELLELFD-LVMMCTNVLN 103

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 115430108  413 FLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGifQAM 492
Cdd:pfam00651   4 LREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEE--NVD 81

                          90       100
                  ....*....|....*....|....*.
gi 115430108  493 CLLICAEMYQVSRLQHICELFIITQL 518
Cdd:pfam00651  82 DLLAAADKLQIPSLVDKCEEFLIKSL 107

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 115430108 406 YNTSLKFFLNKPMLADVVFEI--QGTTVPAHRAILVARCEVMAAMFN-GNYMEAKSVLIPVYGVSKETFLSFLEYLYTDS 482
Cdd:cd18294    1 FAADMKSLINNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRAMFLtGPQKESTQSPLVLSDIEPEVFRAVLEFIYTNC 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 115430108 483 CC--PAGIFQamcLLICAEMYQVSRLQHICELFI 514
Cdd:cd18294   81 VTlsNHTVIE---VLAAAVEYGLDELRKLCERFI 111

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2); RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2) or p83, is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB2 functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108 414 LNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEA--KSVLIPvyGVSKETFLSFLEYLYTDSCCPAGIFQA 491
Cdd:cd18359   15 LAKGTFSDVTFMLDDGTISAHKPLLISSCDWMAAMFGGPFVESstTEVVFP--YTSRSSMRAVLEYLYTGQFSSSPDLDD 92

                         90       100
                 ....*....|....*....|....*..
gi 115430108 492 MCLLICAEMYQVSRLQHICELFIITQL 518
Cdd:cd18359   93 MKLIILANRLCLPHLVALTEQYTVTVL 119

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108 410 LKFFLNkPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIF 489
Cdd:cd18286    9 LQLFLN-GEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVSFVLLFIYGGVLDLPDDV 87

                         90
                 ....*....|..
gi 115430108 490 QAMCLLICAEMY 501
Cdd:cd18286   88 NLGELLSLADMY 99

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 115430108 420 ADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDS---------CCPAGIFQ 490
Cdd:cd18280   15 ADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVFKALLHFIYKDElpddvepagSDSSSLDT 94

                         90       100
                 ....*....|....*....|...
gi 115430108 491 AMC--LLICAEMYQVSRLQHICE 511
Cdd:cd18280   95 TMAqhLLAAADRYALERLRLLCE 117

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 115430108 413 FLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSccpAGIFQ-- 490
Cdd:cd18352    7 YVNNATLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMRFIYTGS---VDITNdi 83

                         90       100
                 ....*....|....*....|....*...
gi 115430108 491 AMCLLICAEMYQVSRLQHICELFIITQL 518
Cdd:cd18352   84 AKDLLRAADQYLLEGLKRLCEYTIAQDL 111

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the 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 115430108 417 PMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVL--IPV---YGVSKETFLSFLEYLYTDsCCPAGIFQA 491
Cdd:cd18296   15 LSFPDVCFQVEGHRFPCHKAFFCGRSDYFKALLRDHFAESEENNgsIPVvtlHDVSPEVFAIVLYYIYTD-DTDLPPENA 93

                         90       100
                 ....*....|....*....|....*...
gi 115430108 492 MCLLICAEMYQVSRLQHICELFIITQLQ 519
Cdd:cd18296   94 YDVLYVADMYLLPGLKRLCGTVLAQSLD 121

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 115430108 420 ADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSC--CPAGIFQamcLLIC 497
Cdd:cd18314    7 SDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQVtlSEENVLD---LLML 83

                         90
                 ....*....|...
gi 115430108 498 AEMYQVSRLQHIC 510
Cdd:cd18314   84 ASKYQVPDLEKLC 96

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2; This family includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108 397 YQARKPlwfyntSLK----FFLNKPMLADVVF----EIQGTTVPAHRAILVARCEVMAAMFNGNyMEAKSVLIPVYGVSK 468
Cdd:cd18281    2 WQASKT------TVKerfaFLFNNETLSDVHFivgkGDNEQRIPAHKFVLSIGSAVFDAMFNGG-MATTSAEIELPDVEP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115430108 469 ETFLSFLEYLYTDSCCpAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQS 520
Cdd:cd18281   75 AAFLALLRFLYSDEVQ-IGPETVMTTLYTAKKYAVPALESACVEFLKKNLSS 125

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115430108 413 FLNkPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYT 480
Cdd:cd18287   17 FLN-EEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKALLKYIYT 83

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 1 (BTBD1); BTBD1, also called Hepatitis C virus NS5A-transactivated protein 8 or HCV NS5A-transactivated protein 8, is a BTB-domain-containing Kelch-like protein that is expressed in skeletal muscle and interacts with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. BTBD1 may serve as substrate-specific adaptor of an E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108 412 FFLNKPMLADVVFEI----------QGTTVPAHRAILVARCEVMAAMFNGNyMEAKSVLIPVYGVSKETFLSFLEYLYTD 481
Cdd:cd18346   15 FLFNNELLSDVRFVVgkgrprgpgpGAQRIPAHRFVLAAGSAVFDAMFNGG-MATTSAEIELPDVEPAAFLALLRFLYSD 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115430108 482 ScCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQS 520
Cdd:cd18346   94 E-VQIGPETVMTTLYTAKKYAVPALEAHCVEFLTKHLRA 131

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108  34 LVSGDES---SLLLNAASTVARPvfTEYQASAFGN--VKLVVHDCPV----WDIFDSDWYTS-RNLI-GGADIIVIKYNV 102
Cdd:cd00157    4 VVVGDGAvgkTCLLISYTTNKFP--TEYVPTVFDNysANVTVDGKQVnlglWDTAGQEEYDRlRPLSyPQTDVFLLCFSV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115430108 103 NDKFSFHEVKDNYIPVIKRALNSVPVIIaaVGT----RQNEELPCTcplcTSDRGSCVSTTEGIQLAKELGAT-YLE 174
Cdd:cd00157   82 DSPSSFENVKTKWYPEIKHYCPNVPIIL--VGTkidlRDDGNTLKK----LEKKQKPITPEEGEKLAKEIGAVkYME 152

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 7 (BTBD7); BTBD7 is a crucial regulator that is essential for region-specific epithelial cell dynamics and branching morphogenesis. It has been implicated in various cancers. BTBD7 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115430108 421 DVVFeiQGTTVPAHRAILVARCEVMAAMFNG--NYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAG 487
Cdd:cd18283    6 DLVF--QGTCFPVHRAILSARCPFFRDLLSSspGYGAEIPVDLPTAGIDVPMFSALLRYLYTGEFGSED 72

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115430108 414 LNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDS 482
Cdd:cd18295   14 LEQGSYSDVTFNVHGESFPAHRCILSARSPYFAEMFETKWKDKREINLKHPLVNPDAFRALLQYLYTGR 82

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 115430108 410 LKFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSccpAGIF 489
Cdd:cd18345    9 LGLLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVMREMLRFIYTGK---APNL 85

                         90       100       110
                 ....*....|....*....|....*....|.
gi 115430108 490 QAMC--LLICAEMYQVSRLQHICELFIITQL 518
Cdd:cd18345   86 DKMAddLLAAADKYALERLKVMCEEALCSNL 116

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6; This family includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108 414 LNKPMLADVVF----EIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKS-VLIPvyGVSKETFLSFLEYLYTDSCCPAGI 488
Cdd:cd18282    2 FNNELMADVHFivgpPGGTQRIPAHKYVLATGSSVFYAMFYGGLAENKNeIEIP--DVEPAAFLNLLRYLYCDEIDLEPD 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 115430108 489 fQAMCLLICAEMYQVSRLQHICELFIITQL 518
Cdd:cd18282   80 -TVLATLYAAKKYLVPHLARACVQFLETSL 108

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115430108 413 FLNKPMLADVVFEIQGTT-VPAHRAILVARCEVMAAMFNgnyMEAKSVLIPVygVSKETFLSFLEYLYT 480
Cdd:cd18299    6 LLHSPSCADVVFILQGGVrIFAHRIVLAAASSVFADLFL---MMTVVTLDSD--ITPEAFRRVLEFLYT 69

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430108 414 LNKPMLADVVFEI--QGTT--VPAHRAILVARCEVMAAMFNGNYMEAKS-VLIPvyGVSKETFLSFLEYLYTDSCCPAGI 488
Cdd:cd18349    3 FNNELMADVHFIVgpPGASqrVPAHKYVLAVGSSVFYAMFYGDLAEVKSeIHIP--DVEPAAFLILLKYMYSDEIDLEAD 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 115430108 489 fQAMCLLICAEMYQVSRLQHICELFIITQL 518
Cdd:cd18349   81 -TVLATLYAAKKYIVPALAKACVNFLETSL 109

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 115430108 420 ADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSccpAGIFQAMC--LLIC 497
Cdd:cd18279   19 TDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGK---APNLDKMAddLLAA 95

                         90
                 ....*....|....
gi 115430108 498 AEMYQVSRLQHICE 511
Cdd:cd18279   96 ADKYALERLKVMCE 109

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115430108 418 MLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYT 480
Cdd:cd18251   22 ILFDVVLVVEGKPIEAHRILLAASCDYFRGMFAGGLREMQQTEVLIHGVSYNAMCKILDFIYT 84