SAP domain of structure-specific endonuclease subunit SLX4 and similar proteins; SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations in the SLX4 gene are found in Fanconi anemia. This model corresponds to a conserved region called the SAP domain, which is responsible for the binding of MUS81, which plays a distinct role in interstrand crosslink repair.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2168985291 1443 PKVPVTPMPRYSIMETPVLKRELDRFGVRALPKRQMVLKLKEIFQYTHQT 1492
Cdd:cd22999      1 KPSPVTPMPDYESMTTPELKKELKKYGFKPLPRKKMIALLEEIWEQTHPY 50

SAP domain of structure-specific endonuclease subunit SLX4 and similar proteins; SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations in the SLX4 gene are found in Fanconi anemia. This model corresponds to a conserved region called the SAP domain, which is responsible for the binding of MUS81, which plays a distinct role in interstrand crosslink repair.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2168985291 1443 PKVPVTPMPRYSIMETPVLKRELDRFGVRALPKRQMVLKLKEIFQYTHQT 1492
Cdd:cd22999      1 KPSPVTPMPDYESMTTPELKKELKKYGFKPLPRKKMIALLEEIWEQTHPY 50

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 2168985291  607 FGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYARCPLliqcvntegFSAVEDGDLTQ----RVLLSDVSSEAAHAFLNYLY 682
Cdd:pfam00651    1 LNELREQGELCDVTLVVG-DKEFRAHKAVLAACSPY---------FKALFSGQESEssvsEITLDDVSPEDFEALLEFMY 70

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168985291  683 TaDTDVPPSLAPDLRSLALRFGVSDLVELCEQ 714
Cdd:pfam00651   71 T-GKLISEENVDDLLAAADKLQIPSLVDKCEE 101

SAP domain of structure-specific endonuclease subunit SLX4 and similar proteins; SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations in the SLX4 gene are found in Fanconi anemia. This model corresponds to a conserved region called the SAP domain, which is responsible for the binding of MUS81, which plays a distinct role in interstrand crosslink repair.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2168985291 1443 PKVPVTPMPRYSIMETPVLKRELDRFGVRALPKRQMVLKLKEIFQYTHQT 1492
Cdd:cd22999      1 KPSPVTPMPDYESMTTPELKKELKKYGFKPLPRKKMIALLEEIWEQTHPY 50

Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found from fungi to mammals. Slx4 with Slx1 acts as a nuclease on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures by cleaving the strand bearing the 5' non-homologous arm at the branch junction and thus generating ligatable nicked products from 5'-flap or replication fork substrates.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985291 1640 EEAVRRYICSQPALHRKVLMYQPLQLAELQAELKQNG--IPVAMGKLLDILDAQCVTFTT 1697
Cdd:pfam09494    1 FEAITELIKSDPSLYEKILTYEPIVLEDLTAWLNEGGflIEVDPGTLKEWCDSQGICFTN 60

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985291  616 LSDVQFQLDsGEVLYAHKFVLYARCPLLiqcvnTEGFSAVEDGDLTQRVLLSDVSSEAAHAFLNYLYTADTDVPPSLAPD 695
Cdd:cd18186      1 LCDVTLVVG-GREFPAHRAVLAARSPYF-----RAMFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELELSEENVEE 74

                   ....*...
gi 2168985291  696 LRSLALRF 703
Cdd:cd18186     75 LLAAADKL 82

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 2168985291  607 FGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYARCPLliqcvntegFSAVEDGDLTQ----RVLLSDVSSEAAHAFLNYLY 682
Cdd:pfam00651    1 LNELREQGELCDVTLVVG-DKEFRAHKAVLAACSPY---------FKALFSGQESEssvsEITLDDVSPEDFEALLEFMY 70

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168985291  683 TaDTDVPPSLAPDLRSLALRFGVSDLVELCEQ 714
Cdd:pfam00651   71 T-GKLISEENVDDLLAAADKLQIPSLVDKCEE 101

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 2168985291  606 DFGAMVNNPHLSDVQFQLDSGEVLYAHKFVLYARCP---LLIqcvntegfsavedGDLTQRVLLSDVSSEAAHAFLNYLY 682
Cdd:cd18299      2 DLRNLLHSPSCADVVFILQGGVRIFAHRIVLAAASSvfaDLF-------------LMMTVVTLDSDITPEAFRRVLEFLY 68

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2168985291  683 TADTDVPPSLAPDLRSLALRFGVSDLVELCEQV 715
Cdd:cd18299     69 TGVLDENEDDLKELKDAAELLELFDLVMMCTNV 101

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 2168985291  611 VNNPHLSDVQFQLdSGEVLYAHKFVLYARCPLLIQCVnTEGFSAVEDgdltQRVLLSDVSSEAAHAFLNYLYTADTDVPP 690
Cdd:cd18314      1 YNDSEFSDVVLCV-GDRKFFAHRIVLCARSPVFRSML-TGSMIESNL----KEVTLEDVEPEIFETVLKYMYTGQVTLSE 74

                           90       100
                   ....*....|....*....|..
gi 2168985291  691 SLAPDLRSLALRFGVSDLVELC 712
Cdd:cd18314     75 ENVLDLLMLASKYQVPDLEKLC 96

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) and similar proteins; This family includes ABTB2, BTBD11, plant ARM repeat protein interacting with ABF2 (ARIA), 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 ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. 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. 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. 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. 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 2168985291  606 DFGAMVNNPHLSDVQFqLDSGEVLYAHKFVLYARCP----LLiqcvnTEGFSaveDGDLTQrVLLSDVSSEAAHAFLNYL 681
Cdd:cd18297      2 IDPHYVNNPEMSDVTF-LVEGRPFYAHKIVLVTASDrfksML-----SSGST---EAQTPV-IEIPDIRYDIFQLMMQYL 71

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2168985291  682 YTADTD---VPPSLAPDLRSLALRFGVSDLVELCE 713
Cdd:cd18297     72 YTGGVEsldVAQDDALELLRAASFFQLDGLKRHCE 106

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. 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 2168985291  618 DVQFQLDSGEVlYAHKFVLYARCPLLIqcvntEGFSAVEDGDLTQRVLLSDVSSEAAHAFLNYLYTADTDVPPSLAPDLR 697
Cdd:cd18306     20 DVILQVGGHEI-PAHRAVLACASPYLF-----ELFSSDSDGESILTVKLDGLDPDAVEVLVNYAYTSRLEVPADLVKSVY 93

                           90
                   ....*....|....*..
gi 2168985291  698 SLALRFGVSDLVELCEQ 714
Cdd:cd18306     94 SAAKKLKMDRVKKACGD 110

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 2168985291  611 VNNPHLSDVQFQLDsGEVLYAHKFVLYArcplliqcvNTEGFSAVEDGDLTQR----VLLSDVSSEAAHAFLNYLYTADT 686
Cdd:cd18352      8 VNNATLSDVTFLVE-GRRFYAHRIALLA---------SSDAFRAMFDGGYREKeardIEIPNIRWEVFELMMRFIYTGSV 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168985291  687 DVPPSLAPDLRSLALRFGVSDLVELCEQVPAT 718
Cdd:cd18352     78 DITNDIAKDLLRAADQYLLEGLKRLCEYTIAQ 109

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 2168985291  608 GAMVNNPHLSDVQFQLdSGEVLYAHKFVLYARCplliqcvntEGFSAVEDGDLTQR----VLLSDVSSEAAHAFLNYLYT 683
Cdd:cd18360      2 GLFFNSPLLADVVFKI-QGTTVPAHRAVLVARC---------EVMAAMFNGNYAEAksflVPIYGVSKDTFLSFLEYLYT 71

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168985291  684 aDTDVPPSL--APDLRSLALRFGVSDLVELCE 713
Cdd:cd18360     72 -DSCCPASIlqAMALLICAEMYQVSRLQHICE 102

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 2168985291  606 DFGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYA-----RCPLLIQCVNTEGFSAVEdgdltqrvLLSDVSSEAAHA-FLN 679
Cdd:cd18292      7 DIAQLYNNEELSDIVLRVG-GKVFHAHRLILAKssdvfRVMLSNDWWSESKQSEIE--------LVEDPECAAVFEkFLR 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2168985291  680 YLYTADTDVPPSLAPDLRSLALRFGVSDLVELCEQ 714
Cdd:cd18292     78 YLYTGQISVNLETALPLLMLADKYNVTDLKQLCVD 112

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985291  616 LSDVQFQLDSGEVlYAHKfvlyarcPLLIqcVNTEGFSAVEDGDLTQ----RVLLSDVSSEAAHAFLNYLYTADTDVPPS 691
Cdd:cd18358     20 FSDVTFKLDDGTI-NAHK-------PLLI--CSCEWMAAMFGGSFIEsansEVVLPNISKVSMQAVLDYLYTKQLSPTAD 89

                           90       100
                   ....*....|....*....|....
gi 2168985291  692 LAP-DLRSLALRFGVSDLVELCEQ 714
Cdd:cd18358     90 LDPlELIALANRFCLPHLVALTEQ 113

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 2168985291  602 LLATDFGAMVNNPHLSDVQFqLDSGEVLYAHKFVLYARCPLliqcvntegFSAVEDGDLTQ----RVLLSDVSSEAAHAF 677
Cdd:cd18279      4 RLAEDLGNLWENSRFTDCCL-CVGGQEFQAHKAILAARSPV---------FSAMFEHEMEEskknRVEINDVDPEVFKEM 73

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2168985291  678 LNYLYTADTDVPPSLAPDLRSLALRFGVSDLVELCEQV 715
Cdd:cd18279     74 MRFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDA 111

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 2168985291  603 LATDFGAMVNNPHLSDVQFQLdSGEVLYAHKFVLYARCPLliqcvntegFSAVEDGDLTQ----RVLLSDVSSEAAHAFL 678
Cdd:cd18343      8 LAEDLGNLWENSRFTDCSLFV-GGQEFKAHKSILAARSPV---------FNAMFEHEMEEskknRVEINDVDPEVFKEMM 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2168985291  679 NYLYTADTDVPPSLAPDLRSLALRFGVSDLVELCEQ 714
Cdd:cd18343     78 RFIYTGKAPNLDKMADNLLAAADKYALERLKVMCEE 113

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 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        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985291  606 DFGAMVNNPHLSDVQFQL-DSGEVLYAHKFVLYARCPLLI---------------QCVNTEGFSAVEDGDLTQR-----V 664
Cdd:cd18308     13 DFGRLLESRQFCDVEFIVgEEEERIPAHIAFVAARSKWLRnkilqarerqkqkaeQEVEDEGSEADSSSASKNDspmleV 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168985291  665 LLSDVSSEAAHAFLNYLYT-----ADTDVPP------SLAPDLRSLALRFGVSDLVELCEQ 714
Cdd:cd18308     93 RLPEADPEAFELILSFIYTdkidpTRKGQDPgsnevvLLMMDVYRLALQFQMSRLEQLCVQ 153

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in glial cell line-derived neurotrophic factor-inducible zinc finger protein 1 (GZF1); GZF1 is also called GDNF-inducible zinc finger protein 1, zinc finger and BTB domain-containing protein 23 (ZBTB23), or zinc finger protein 336 (ZNF336). It is a sequence-specific transcriptional repressor that binds the GZF1 responsive element (GRE), with the consensus sequence of 5'-TGCGCN[TG][CA]TATA-3'. It may play a role in renal branching morphogenesis. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985291  615 HLSDVQFQLD---SGEVLYAHKFVLYARCPLLIQCVNTEgfsAVEDGDLTQrVLLSDVSSEAAHAFLNYLYTADTDVPPS 691
Cdd:cd18211     24 HLCDVTVQVEhqgSKEEFSAHKAVLAASSKYFKEVFLNE---KISDGKNTN-VMLNEIYTADFASFLEFVYTAKVEVEED 99

                           90       100
                   ....*....|....*....|....*.
gi 2168985291  692 LAPDLRSLALRFGVSDLVELCEQVPA 717
Cdd:cd18211    100 RVQRMLEIAEKLKCLDLSETCFQLKK 125

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 2168985291  618 DVQFQLDSgevlyaHKFvlyaRCPLLIQCVNTEGFSAVEDGDLTQR---------VLLSDVSSEAAHAFLNYLYTADTDV 688
Cdd:cd18296     19 DVCFQVEG------HRF----PCHKAFFCGRSDYFKALLRDHFAESeenngsipvVTLHDVSPEVFAIVLYYIYTDDTDL 88

                           90
                   ....*....|..
gi 2168985291  689 PPSLAPDLRSLA 700
Cdd:cd18296     89 PPENAYDVLYVA 100

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 2168985291  602 LLATDFGAMVNNPHLSDVQFqLDSGEVLYAHKFVLYARCPLliqcvntegFSAVEDGDLTQR----VLLSDVSSEAAHAF 677
Cdd:cd18344      9 MLTDDLGELWENSLFTDCCL-LVAGHEFRAHKAILAARSPV---------FRAMFEHEMEERlknpIEIHDLDPQVFKEM 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2168985291  678 LNYLYT--ADTDVPPSLAPDLRSLALRFGVSDLVELCEQV 715
Cdd:cd18344     79 MGFIYTgkAPHLHSHSMACDVLAAADKYGLEGLKVLCEDA 118