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 568995794 1368 PKVPITPMPRYSIMETPVLKKELDRFGVRALPKRQMVLKLKEIFQYTHQT 1417
Cdd:cd22999     1 KPSPVTPMPDYESMTTPELKKELKKYGFKPLPRKKMIALLEEIWEQTHPY 50

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995794  608 LYMADTDMPPSLVPDLRSLALRFGV--SDLV---QLCEQVPAVVDLEGEQPEETSEDCESRAETFLELLRSVWVDNEEEV 682
Cdd:PLN02372  320 VYTRSSTLPESIVPELEKAAKKVGRdfSDFVrtdNTCGPEPPLLERLEKDVEEGEKTIVKEARQIEEELEKEVEKLGKEE 399

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568995794  683 ETLLKPELCEEERERVNEAEMEEIYEFAATQRKLLQ 718
Cdd:PLN02372  400 ESLFKRVALEEGLKELEQDEENFLKELSKEEKELLE 435

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 568995794 1368 PKVPITPMPRYSIMETPVLKKELDRFGVRALPKRQMVLKLKEIFQYTHQT 1417
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 568995794   534 FGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYARCPlliqYVSTeSFSSEEDGDLTQRALLSDVSSEAAHAFLNYLYmADT 613
Cdd:pfam00651    1 LNELREQGELCDVTLVVG-DKEFRAHKAVLAACSP----YFKA-LFSGQESESSVSEITLDDVSPEDFEALLEFMY-TGK 73

                           90       100
                   ....*....|....*....|....*...
gi 568995794   614 DMPPSLVPDLRSLALRFGVSDLVQLCEQ 641
Cdd:pfam00651   74 LISEENVDDLLAAADKLQIPSLVDKCEE 101

violaxanthin de-epoxidase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995794  608 LYMADTDMPPSLVPDLRSLALRFGV--SDLV---QLCEQVPAVVDLEGEQPEETSEDCESRAETFLELLRSVWVDNEEEV 682
Cdd:PLN02372  320 VYTRSSTLPESIVPELEKAAKKVGRdfSDFVrtdNTCGPEPPLLERLEKDVEEGEKTIVKEARQIEEELEKEVEKLGKEE 399

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568995794  683 ETLLKPELCEEERERVNEAEMEEIYEFAATQRKLLQ 718
Cdd:PLN02372  400 ESLFKRVALEEGLKELEQDEENFLKELSKEEKELLE 435

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 568995794 1368 PKVPITPMPRYSIMETPVLKKELDRFGVRALPKRQMVLKLKEIFQYTHQT 1417
Cdd:cd22999     1 KPSPVTPMPDYESMTTPELKKELKKYGFKPLPRKKMIALLEEIWEQTHPY 50

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 568995794  537 MVNNPHLSDVQFQLDSGEVlYAHKFVLYARCPLLIQYVS---TESFSSEEDgdltqralLSDVSSEAAHAFLNYLYmadT 613
Cdd:cd18300     3 FLNKGLFSDVTFIVEDGTI-PAHKALLVARCDVMAAMFGgnfRESSAKEVE--------LPGVSKETFLALLEYLY---T 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568995794  614 DMPPSL----VPDLRSLALRFGVSDLVQLCEQV 642
Cdd:cd18300    71 DQAPILedgdCVGLIVLANRLCLPRLVALCEQY 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 568995794   534 FGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYARCPlliqYVSTeSFSSEEDGDLTQRALLSDVSSEAAHAFLNYLYmADT 613
Cdd:pfam00651    1 LNELREQGELCDVTLVVG-DKEFRAHKAVLAACSP----YFKA-LFSGQESESSVSEITLDDVSPEDFEALLEFMY-TGK 73

                           90       100
                   ....*....|....*....|....*...
gi 568995794   614 DMPPSLVPDLRSLALRFGVSDLVQLCEQ 641
Cdd:pfam00651   74 LISEENVDDLLAAADKLQIPSLVDKCEE 101

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 568995794    545 DVQFQLDsGEVLYAHKFVLYARCPLLiqyvsTESFSSEEDGDLTQRALLSDVSSEAAHAFLNYLYMADTDMPPSLVPDLR 624
Cdd:smart00225    1 DVTLVVG-GKKFHAHKAVLAAHSPYF-----KALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELL 74

                            90
                    ....*....|....*..
gi 568995794    625 SLALRFGVSDLVQLCEQ 641
Cdd:smart00225   75 ELADYLQIPGLVELCEE 91

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 568995794  538 VNNPHLSDVQFQLdSGEVLYAHKFVLYARCPLLIQYVSTESFSSEEdgdltQRALLSDVSSEAAHAFLNYLYMADTDMPP 617
Cdd:cd18314     1 YNDSEFSDVVLCV-GDRKFFAHRIVLCARSPVFRSMLTGSMIESNL-----KEVTLEDVEPEIFETVLKYMYTGQVTLSE 74

                          90       100
                  ....*....|....*....|..
gi 568995794  618 SLVPDLRSLALRFGVSDLVQLC 639
Cdd:cd18314    75 ENVLDLLMLASKYQVPDLEKLC 96

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1); RCBTB1 is also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), CLL deletion region gene 7 protein, regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5. It is a novel chromosome condensation regulator-like guanine nucleotide exchange factor that may be involved in cell cycle regulation by chromatin remodeling. It may also function as a tumor suppressor that regulates pathways of DNA damage/repair and apoptosis. RCBTB1 may also be a substrate adaptor for a cullin3 (CUL3) E3 ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Biallelic mutations in RCBTB1 may cause isolated and syndromic retinal dystrophy. 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 568995794  539 NNPHLSDVQFQLDsGEVLYAHKFVLYARCplliQYVST--ESFSSEEDGDLTQralLSDVSSEAAHAFLNYLYMADTDMP 616
Cdd:cd18353    16 DSPETSDLKFRVD-GKYIHVHKAVLKIRC----EHFRTmfQSHWNEDMKEVIE---IDQFSYPVYRAFLEYLYTDSVDLP 87

                          90       100
                  ....*....|....*....|....*.
gi 568995794  617 PSLVPDLRSLALRFGVSDLVQLCEQV 642
Cdd:cd18353    88 PEDAIGLLDLATSYCENRLKKLCQHI 113

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 568995794  527 LGLLVTDFGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYARCplliQYVST-------ESFSSEedgdltqrALLSDVSSE 599
Cdd:cd18287     6 VHFLSEDIGALFLNEEYSDVTFVVE-EKRFPAHRVILAARS----EYFRAllyggmrESQQSE--------IELKDTNAE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568995794  600 AAHAFLNYLY---MADTDMPPSLVPDLRSLALRFGVSDLVQL 638
Cdd:cd18287    73 AFKALLKYIYtgrLTLTDLKEDVLLDVLGLAHQYGFEELEAA 114

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 568995794  533 DFGAMVNNPHLSDVQFqLDSGEVLYAHKFVLYARCPLLIQYVSteSFSSEEDGDLTQralLSDVSSEAAHAFLNYLYMAD 612
Cdd:cd18297     2 IDPHYVNNPEMSDVTF-LVEGRPFYAHKIVLVTASDRFKSMLS--SGSTEAQTPVIE---IPDIRYDIFQLMMQYLYTGG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568995794  613 TD---MPPSLVPDLRSLALRFGVSDLVQLCE 640
Cdd:cd18297    76 VEsldVAQDDALELLRAASFFQLDGLKRHCE 106

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 568995794  535 GAMVNNPHLSDVQFQLdSGEVLYAHKFVLYARCPLLI-----QYVSTESFSSEEDGdltqrallsdVSSEAAHAFLNYLY 609
Cdd:cd18360     2 GLFFNSPLLADVVFKI-QGTTVPAHRAVLVARCEVMAamfngNYAEAKSFLVPIYG----------VSKDTFLSFLEYLY 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568995794  610 mADTDMPPSLVPDLRSL--ALRFGVSDLVQLCE 640
Cdd:cd18360    71 -TDSCCPASILQAMALLicAEMYQVSRLQHICE 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 568995794  530 LVTDFGAMVNNPHLSDVQFQLDsGEVLYAHKFVLYARCPLLIQYVSTESFSSEEDGDLTqraLLSDVSSEAAHA-FLNYL 608
Cdd:cd18292     4 FLQDIAQLYNNEELSDIVLRVG-GKVFHAHRLILAKSSDVFRVMLSNDWWSESKQSEIE---LVEDPECAAVFEkFLRYL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568995794  609 YMADTDM-PPSLVPDLRsLALRFGVSDLVQLCEQ 641
Cdd:cd18292    80 YTGQISVnLETALPLLM-LADKYNVTDLKQLCVD 112

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 568995794  538 VNNPHLSDVQFqLDSGEVLYAHKFVLYARCPlliQYVSTESFSSEEDGDLTQRALLSDVSSEAAHAFLNYLYMADTD--- 614
Cdd:cd18350    19 LNNKEMSDVTF-LVEGKLFYAHKVLLVTASN---RFKSLLTNKSEQESQGSKTIEISDIKYHIFQMLMQYLYYGGTEsme 94

                          90       100
                  ....*....|....*....|....*.
gi 568995794  615 MPPSLVPDLRSLALRFGVSDLVQLCE 640
Cdd:cd18350    95 IPIADVLELLSAASLFQLDALQRHCE 120

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 41 (KLHL41); KLHL41 is also called Kel-like protein 23, Kelch repeat and BTB domain-containing protein 10 (KBTBD10), Kelch-related protein 1 (Krp1), or sarcosine. It is a novel kelch-related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. 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 568995794  559 HKFVLYARCPLLIQYvstesFSSEEDGDLTQRALLSDVSSEAAHAFLNYLYMADTDMPPSLVPDLRSLALRFGVSDLVQL 638
Cdd:cd18341    42 HRLILAACSPYFREY-----FLSEESEEKKKEVVLDNVDPNIMDMILKYLYSAEIDLNDGNVQDIFALASRFQIPSVFTV 116

                  .
gi 568995794  639 C 639
Cdd:cd18341   117 C 117

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant regulatory proteins, NPR1-4, and similar proteins; NPR1 and NPR2 are essential for pathogenicity and the utilization of many nitrogen sources. NPR1 is also called nitrogen pathogenicity regulation protein NPR1, non-inducible immunity protein 1 (Nim1), nonexpresser of PR genes 1, or salicylic acid insensitive 1 (Sai1). It acts as a transcription coactivator that plays dual roles in regulating plant immunity. NPR3 and NPR4 are involved in negative regulation of defense responses against pathogens in plant. NPR proteins contain a BTB domain, DUF3420, ankyrin (ANK) repeats, and a conserved C-terminal 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 568995794  528 GLLVTDFGAMVNNPHL--SDVQFQLDSGEVLYAHKFVLYARCPLLIQYVSTESFSSEEDG-DLTQRALLSD--VSSEAAH 602
Cdd:cd18310     1 KKLSSDLENLLDSPDLfySDAEIIVEGGRPVPVHRCILAARSPFFRDIFASAKAEGANTKpKLELRELIPGgiVGYDAFM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568995794  603 AFLNYLYMADTDMPPSLVP--------------------DLRSLALRFGVSDLVQLCEQ 641
Cdd:cd18310    81 LVLSYLYSGRLRLVPKEGSacvdsdcwhvacrpavdfalEVLYAASVFQIPELVSLFQR 139

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568995794  545 DVQFQLDsGEVLYAHKFVLYARCPLLIQYVSTESFSSeEDGDLTQRALLSDVSSEAAHAFLNYLYMADTDMP 616
Cdd:cd18301    20 DVVFQVG-GKTFPAHKFILASRSDYFRKLFLSSLLTS-EDAVGCDVVHIEKVPPEIFEQLLQFIYTDTCDLL 89

violaxanthin de-epoxidase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995794  608 LYMADTDMPPSLVPDLRSLALRFGV--SDLV---QLCEQVPAVVDLEGEQPEETSEDCESRAETFLELLRSVWVDNEEEV 682
Cdd:PLN02372  320 VYTRSSTLPESIVPELEKAAKKVGRdfSDFVrtdNTCGPEPPLLERLEKDVEEGEKTIVKEARQIEEELEKEVEKLGKEE 399

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568995794  683 ETLLKPELCEEERERVNEAEMEEIYEFAATQRKLLQ 718
Cdd:PLN02372  400 ESLFKRVALEEGLKELEQDEENFLKELSKEEKELLE 435