WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  381 HPNWCQQVKYIPQLNVVASCSAVEKsslvlIILPGKEPEKPRLSSLNLRKGILCFDYCPDRNFLATGGYDPHIRLWNpLV 460
Cdd:cd00200      8 HTGGVTCVAFSPDGKLLATGSGDGT-----IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-LE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  461 SKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTLICSTYN 540
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNSVAFSPDGTFVASSSQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  541 IGILRGY-LESQGPLKTgrMTTHNTPLCAVLYSKIFKQVVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQS 619
Cdd:cd00200    156 DGTIKLWdLRTGKCVAT--LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH---ENGVNSVAFSPD 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1681253214  620 ERCLLTGLRDGTMQMWNYNTGECLMTFPNPDRvEISGIVHMN--KVFYTTGWSKRI 673
Cdd:cd00200    231 GYLLASGSEDGTIRVWDLRTGECVQTLSGHTN-SVTSLAWSPdgKRLASGSADGTI 285

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681253214 1232 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 1290
Cdd:cd21577      3 VKTDMETSFYSPSHSqlepvdlSLSKRSSPPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPP 68

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  381 HPNWCQQVKYIPQLNVVASCSAVEKsslvlIILPGKEPEKPRLSSLNLRKGILCFDYCPDRNFLATGGYDPHIRLWNpLV 460
Cdd:cd00200      8 HTGGVTCVAFSPDGKLLATGSGDGT-----IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-LE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  461 SKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTLICSTYN 540
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNSVAFSPDGTFVASSSQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  541 IGILRGY-LESQGPLKTgrMTTHNTPLCAVLYSKIFKQVVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQS 619
Cdd:cd00200    156 DGTIKLWdLRTGKCVAT--LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH---ENGVNSVAFSPD 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1681253214  620 ERCLLTGLRDGTMQMWNYNTGECLMTFPNPDRvEISGIVHMN--KVFYTTGWSKRI 673
Cdd:cd00200    231 GYLLASGSEDGTIRVWDLRTGECVQTLSGHTN-SVTSLAWSPdgKRLASGSADGTI 285

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1681253214   461 SKKPVWLMKGHQTSVTHLLVNSrNASILISISRDKNIRVWD 501
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40

WD domain, G-beta repeat;

                           10        20
                   ....*....|....*....|....*....
gi 1681253214  429 RKGILCFDYCPDRNFLATGGYDPHIRLWN 457
Cdd:pfam00400   11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  381 HPNWCQQVKYIPQLNVVASCSAVEKsslvlIILPGKEPEKPRLSSLNLRKGILCFDYCPDRNFLATGGYDPHIRLWNpLV 460
Cdd:cd00200      8 HTGGVTCVAFSPDGKLLATGSGDGT-----IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-LE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  461 SKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTLICSTYN 540
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNSVAFSPDGTFVASSSQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  541 IGILRGY-LESQGPLKTgrMTTHNTPLCAVLYSKIFKQVVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQS 619
Cdd:cd00200    156 DGTIKLWdLRTGKCVAT--LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH---ENGVNSVAFSPD 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1681253214  620 ERCLLTGLRDGTMQMWNYNTGECLMTFPNPDRvEISGIVHMN--KVFYTTGWSKRI 673
Cdd:cd00200    231 GYLLASGSEDGTIRVWDLRTGECVQTLSGHTN-SVTSLAWSPdgKRLASGSADGTI 285

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  431 GILCFDYCPDRNFLATGGYDPHIRLWNpLVSKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQS 510
Cdd:COG2319    206 AVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAF-SPDGRLLASGSADGTVRLWDLATGELLRT 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  511 FCGklfplGNCPITSTYFYRSSTLICSTYNIGILRGY-LESQGPLKTgrMTTHNTPLCAVLYSKIFKQVVSGCLQGLVSV 589
Cdd:COG2319    284 LTG-----HSGGVNSVAFSPDGKLLASGSDDGTVRLWdLATGKLLRT--LTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1681253214  590 WDISTGKkrmEIPVSGIQESELTAMALDQSERCLLTGLRDGTMQMWN 636
Cdd:COG2319    357 WDLATGE---LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  303 DSCVMVMDYWTDCHKAVFCygdtkgNATIFISDnVAGGLFNPQILprASKWDHwfTVSLKKLlnEKAPLYRSFRMkglHP 382
Cdd:cd00200     30 DGTIKVWDLETGELLRTLK------GHTGPVRD-VAASADGTYLA--SGSSDK--TIRLWDL--ETGECVRTLTG---HT 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  383 NWCQQVKYIPQLNVVASCSA--------VEKSSLVlIILPGKEpekprlsslnlrKGILCFDYCPDRNFLATGGYDPHIR 454
Cdd:cd00200     94 SYVSSVAFSPDGRILSSSSRdktikvwdVETGKCL-TTLRGHT------------DWVNSVAFSPDGTFVASSSQDGTIK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  455 LWNpLVSKKPVWLMKGHQTSVTHLLVNSRNASILISiSRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTL 534
Cdd:cd00200    161 LWD-LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS-SSDGTIKLWDLSTGKCLGTLRGH-----ENGVNSVAFSPDGYL 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1681253214  535 ICSTYNIGILRGY-LESQGPLKTGRMttHNTPLCAVLYSKIFKQVVSGCLQGLVSVWD 591
Cdd:cd00200    234 LASGSEDGTIRVWdLRTGECVQTLSG--HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  431 GILCFDYCPDRNFLATGGYDPHIRLWNpLVSKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQS 510
Cdd:COG2319    248 SVRSVAFSPDGRLLASGSADGTVRLWD-LATGELLRTLTGHSGGVNSVAF-SPDGKLLASGSDDGTVRLWDLATGKLLRT 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681253214  511 FCGKlfplgNCPITSTYFYRSSTLICSTYNIGILRGY-LESQGPLKTgrMTTHNTPLCAVLYSKIFKQVVSGCLQGLVSV 589
Cdd:COG2319    326 LTGH-----TGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRT--LTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398

                   ....*
gi 1681253214  590 WDIST 594
Cdd:COG2319    399 WDLAT 403

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1681253214   461 SKKPVWLMKGHQTSVTHLLVNSrNASILISISRDKNIRVWD 501
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                            10        20
                    ....*....|....*....|....*....
gi 1681253214   429 RKGILCFDYCPDRNFLATGGYDPHIRLWN 457
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681253214 1232 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 1290
Cdd:cd21577      3 VKTDMETSFYSPSHSqlepvdlSLSKRSSPPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPP 68