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 568988822 350 HEDFLTVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLY 429
Cdd:cd18353    1 HDDFLTVAESLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYPVYRAFLEYLY 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568988822 430 TDTVDLPPEDAIGLLDLATSYCENRLKRLCQHIIKRG 466
Cdd:cd18353   81 TDSVDLPPEDAIGLLDLATSYCENRLKKLCQHIIKRG 117

BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1); RCBTB1, also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), or CLL deletion region gene 7 protein, or regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5, is a novel chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) 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. Moreover, RCBTB1 acts as a putative 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568988822 466 GITVENAFSLFSAAVRYDAEDLEEFCFKFCINHLTEVTQTAAFWQMDGPLLKEFIAKASKCGAFKN 531
Cdd:cd18528    1 GITVENAFSLLSAAVRYDAEDLEEFCFKFCVNHLTEVTQTAAFWQMDGNLLKEFIAKASKCGAFKN 66

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 568988822 350 HEDFLTVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLY 429
Cdd:cd18353    1 HDDFLTVAESLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYPVYRAFLEYLY 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568988822 430 TDTVDLPPEDAIGLLDLATSYCENRLKRLCQHIIKRG 466
Cdd:cd18353   81 TDSVDLPPEDAIGLLDLATSYCENRLKKLCQHIIKRG 117

BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1); RCBTB1, also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), or CLL deletion region gene 7 protein, or regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5, is a novel chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) 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. Moreover, RCBTB1 acts as a putative 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568988822 466 GITVENAFSLFSAAVRYDAEDLEEFCFKFCINHLTEVTQTAAFWQMDGPLLKEFIAKASKCGAFKN 531
Cdd:cd18528    1 GITVENAFSLLSAAVRYDAEDLEEFCFKFCVNHLTEVTQTAAFWQMDGNLLKEFIAKASKCGAFKN 66

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 568988822  360 LKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVdLPPED 439
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKL-ISEEN 79

                          90       100
                  ....*....|....*....|....*
gi 568988822  440 AIGLLDLATSYCENRLKRLCQHIIK 464
Cdd:pfam00651  80 VDDLLAAADKLQIPSLVDKCEEFLI 104

kelch-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822 374 FRIDGKYIHVHKAVLKIRCEHFRSMFQSywNEDMKEVIEidQFSYPVYRAFLQYLYTDTVDLPPEDAIGLLDLATSYCEN 453
Cdd:PHA03098  16 IVNGGGIIKVHKIILSSSSEYFKKMFKN--NFKENEINL--NIDYDSFNEVIKYIYTGKINITSNNVKDILSIANYLIID 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568988822 454 RLKRLCQHIIKRGITVENAFSLFSAAVRYDAEDLEEFCFKFCINHLT 500
Cdd:PHA03098  92 FLINLCINYIIKIIDDNNCIDIYRFSFFYGCKKLYSAAYNYIRNNIE 138

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 568988822 350 HEDFLTVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLY 429
Cdd:cd18353    1 HDDFLTVAESLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYPVYRAFLEYLY 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568988822 430 TDTVDLPPEDAIGLLDLATSYCENRLKRLCQHIIKRG 466
Cdd:cd18353   81 TDSVDLPPEDAIGLLDLATSYCENRLKKLCQHIIKRG 117

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822  37 VTDNDEVFVFGLNYSNCLGTGDNQSTLVPKKLEALCGkkIKSLSYGSGpHVLLTTEDGVVYAWGHNGYSQLGNGTTNQGI 116
Cdd:COG5184   13 LKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGD-HTCALKADGTVWCWGNNSYGQLGDGTTTDRT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822 117 APVQVCTnllIKQVIEVACGSHHSMALAADGELFAWGYNNCGQVGSGSTANQPTPRKVTNCLHTkrVVNIACGQTSSMAV 196
Cdd:COG5184   90 TPVKVPG---LTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSG--VVAIAAGGYHTCAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822 197 LDSGEVYGWGYNGNGQLGLGNNGNQLTPVRVAALHGmcVNQIVCGYAHTLALTDEGLLYAWGANTYGQLGTGSKNNLLSP 276
Cdd:COG5184  165 KSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATP 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568988822 277 TQImVEKERVIEIAAchSTHTSAAKTQGGHVYMWGQ 312
Cdd:COG5184  243 VQV-AGLTGVVAIAA--GGSHTCALKSDGTVWCWGD 275

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822  37 VTDNDEVFVFGLNYSNCLGTGDNQSTLVPKKLeALCGKKIKSLSYGSGpHVLLTTEDGVVYAWGHNGYSQLGNGTTNQGI 116
Cdd:COG5184  113 LKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGY-HTCALKSDGTVWCWGANSYGQLGDGTTTDRP 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822 117 APVQVCTnllIKQVIEVACGSHHSMALAADGELFAWGYNNCGQVGSGSTANQPTPRKVTNclhTKRVVNIACGQTSSMAV 196
Cdd:COG5184  191 TPVQVGG---LSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAG---LTGVVAIAAGGSHTCAL 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988822 197 LDSGEVYGWGYNGNGQLGLGNNGNQLTPVRVAALHGmcVNQIVCGYAHTLALTDEGLLYAWGANTYGQLGTGSKNNLLSP 276
Cdd:COG5184  265 KSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTP 342

                 .
gi 568988822 277 T 277
Cdd:COG5184  343 V 343

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 568988822 351 EDFLTVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFqsywNEDMKEVIEIDQFSYPVYRAFLQYLYT 430
Cdd:cd18354    2 DDHLTVAESLKREFDNPDTADLKFLVDGKYIYVHKVLLKIRCEHFRSLL----NENEEEIIEMSQFSYPVYRAFLEYLYT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568988822 431 DTVDLPPEDAIGLLDLATSYCENRLKRLCQHIIKRGITVE 470
Cdd:cd18354   78 DSISLSPEDAIGLLDLATFYRENRLKKLCQQTIKQGICEE 117

BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1); RCBTB1, also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), or CLL deletion region gene 7 protein, or regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5, is a novel chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) 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. Moreover, RCBTB1 acts as a putative 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568988822 466 GITVENAFSLFSAAVRYDAEDLEEFCFKFCINHLTEVTQTAAFWQMDGPLLKEFIAKASKCGAFKN 531
Cdd:cd18528    1 GITVENAFSLLSAAVRYDAEDLEEFCFKFCVNHLTEVTQTAAFWQMDGNLLKEFIAKASKCGAFKN 66

BACK (BTB and C-terminal Kelch) domain found in RCC1 and BTB domain-containing protein 2 (RCBTB2); RCBTB2, also called chromosome condensation 1-like (CHC1-L), or RCC1-like G exchanging factor, or regulator of chromosome condensation and BTB domain-containing protein 2, is a chromosome condensation regulator-like guanine nucleotide exchange factor (GEF) protein for the Ras-related GTPase Ran.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988822 467 ITVENAFSLFSAAVRYDAEDLEEFCFKFCINHLTEVTQTAAFWQMDGPLLKEFIAKASKCGAFKN 531
Cdd:cd18529    1 ISEENAIALLSAAVKYEAQDLEEFCFKFCINHMTVVTQTQAFADMDHDLLKNFISKASKVGAFKN 65

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 568988822   371 DLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDLPPEDAIGLLDLATSY 450
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYL 80

                           90
                   ....*....|....*..
gi 568988822   451 CENRLKRLCQHIIKRGI 467
Cdd:smart00225  81 QIPGLVELCEEFLLKLL 97

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 568988822  360 LKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVdLPPED 439
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKL-ISEEN 79

                          90       100
                  ....*....|....*....|....*
gi 568988822  440 AIGLLDLATSYCENRLKRLCQHIIK 464
Cdd:pfam00651  80 VDDLLAAADKLQIPSLVDKCEEFLI 104

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 568988822 357 AESLKKEFDSPETADLKFRI--DGKYIHVHKAVLKIRCEHFRSMF-QSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTV 433
Cdd:cd18294    2 AADMKSLINNPEFSDVKFLVgpERQEIFAHKCILAARCEVFRAMFlTGPQKESTQSPLVLSDIEPEVFRAVLEFIYTNCV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 568988822 434 DLPPEDAIGLLDLATSYCENRLKRLCQHII 463
Cdd:cd18294   82 TLSNHTVIEVLAAAVEYGLDELRKLCERFI 111

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 568988822 365 DSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDLPPEDAIGLL 444
Cdd:cd18352    9 NNATLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMRFIYTGSVDITNDIAKDLL 88

                         90       100
                 ....*....|....*....|....*..
gi 568988822 445 DLATSYCENRLKRLCQHIIKRGITVEN 471
Cdd:cd18352   89 RAADQYLLEGLKRLCEYTIAQDLTLEN 115

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 568988822 355 TVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQS-YWNEDMKEVIEI--DQFSYPVYRAFLQYLYTD 431
Cdd:cd18292    3 EFLQDIAQLYNNEELSDIVLRVGGKVFHAHRLILAKSSDVFRVMLSNdWWSESKQSEIELveDPECAAVFEKFLRYLYTG 82

                         90       100
                 ....*....|....*....|....*....
gi 568988822 432 TVDLPPEDAIGLLDLATSYCENRLKRLCQ 460
Cdd:cd18292   83 QISVNLETALPLLMLADKYNVTDLKQLCV 111

Regulator of chromosome condensation (RCC1) repeat;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568988822  199 SGEVYGWGYNGNGQLGLGNNGNQLTPVRVAALHGMCVNQIVCGYAHTLAL 248
Cdd:pfam00415   1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and 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, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988822 373 KFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDLPPEDAIGLLDLA 447
Cdd:cd01165    2 VLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDASNLLELLEAA 76

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 568988822 348 VEHEDFLtvAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQY 427
Cdd:cd18287    3 IDHVHFL--SEDIGALFLNEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKALLKY 80

                         90       100
                 ....*....|....*....|....*..
gi 568988822 428 LYTDTVDL--PPEDAI-GLLDLATSYC 451
Cdd:cd18287   81 IYTGRLTLtdLKEDVLlDVLGLAHQYG 107

Regulator of chromosome condensation (RCC1) repeat;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568988822   93 DGVVYAWGHNGYSQLGNGTTNQGIAPVQVcTNLLIKQVIEVACGSHHSMAL 143
Cdd:pfam00415   1 DGRVYTWGRNDYGQLGLGTTENVLVPQKV-EGLSGNKVVQVACGGDHTVAL 50

Regulator of chromosome condensation (RCC1) repeat;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568988822  251 EGLLYAWGANTYGQLGTGSKNNLLSPTQIMVEKERVIEIAACHSTHTSA 299
Cdd:pfam00415   1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49

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 568988822 356 VAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDL 435
Cdd:cd18345    5 LSDDLGLLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVMREMLRFIYTGKAPN 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568988822 436 PPEDAIGLLDLATSYCENRLKRLCQHIIKRGITVENA 472
Cdd:cd18345   85 LDKMADDLLAAADKYALERLKVMCEEALCSNLSVENV 121

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 568988822 356 VAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDL 435
Cdd:cd18343    8 LAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGKAPN 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568988822 436 PPEDAIGLLDLATSYCENRLKRLCQHIIKRGITVEN 471
Cdd:cd18343   88 LDKMADNLLAAADKYALERLKVMCEEALCNNLSVEN 123

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 568988822 358 ESLkkeFDSPET--ADLKFRID-GKYIHVHKAVLKIRCEHFRSMFQSYWNE--------DMKEVIEIDQFSYPVYRAFLQ 426
Cdd:cd18310    8 ENL---LDSPDLfySDAEIIVEgGRPVPVHRCILAARSPFFRDIFASAKAEgantkpklELRELIPGGIVGYDAFMLVLS 84

                         90
                 ....*....|....*....
gi 568988822 427 YLYTDTVDLPPEDAIGLLD 445
Cdd:cd18310   85 YLYSGRLRLVPKEGSACVD 103

BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal to a BTB domain, in a diverse set of architectures together with Kelch, MATH, and/or TAZ domains. It is involved in interactions with the Cullin3 (Cul3) ubiquitin ligase complex, as well as in homo-oligomerization. Most proteins containing the BACK domain are understood to function as adaptor proteins that play a role in ubiquitination of various substrates.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568988822 468 TVENAFSLFSAAVRYDAEDLEEFCFKFCINHLTEVTQTAAFWQMDGPLLKEFIA 521
Cdd:cd14733    1 DPENCLGILELADLYNLEELKEKALKFILENFEEVSKSEEFLELSVELLLELLS 54

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 568988822 355 TVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTV- 433
Cdd:cd18344    9 MLTDDLGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEERLKNPIEIHDLDPQVFKEMMGFIYTGKAp 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568988822 434 DLPPED-AIGLLDLATSYCENRLKRLCQHIIKRGITVENA 472
Cdd:cd18344   89 HLHSHSmACDVLAAADKYGLEGLKVLCEDALCRNLSVENA 128

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 568988822 370 ADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDLPPEDAIGLLDLATS 449
Cdd:cd18272   33 ADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARNRVIELKDVSESVFQLLVDYIYHGTVKLRVEELQETYEVADM 112

                         90       100
                 ....*....|....*....|..
gi 568988822 450 YCENRLKRLCQHIIKRGITVEN 471
Cdd:cd18272  113 YQLTALFEECSRFLARTVQVRN 134

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP); SPOP, also called HIB homolog 1 or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins, such as BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. 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 568988822 356 VAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDL 435
Cdd:cd18342    9 LADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPN 88