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 568919737  44 GLVFSRGEVLSGADNTARQRTRETQVVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTM 123
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGH---TSYVSSVAFSPDGRILSSSSRDKTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737 124 QMWNYNTGECLMTFPNPDRVEISGIVHMNKVFYTTGWSK---RITNFTFQKITQALscyhwqSFHTEDILSMDKY-QNQF 199
Cdd:cd00200  118 KVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgtiKLWDLRTGKCVATL------TGHTGEVNSVAFSpDGEK 191

                        170       180       190
                 ....*....|....*....|....*....|
gi 568919737 200 LGTSSYNGDIVFWNVSTSKPILSFNASKSP 229
Cdd:cd00200  192 LLSSSSDGTIKLWDLSTGKCLGTLRGHENG 221

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 568919737  44 GLVFSRGEVLSGADNTARQRTRETQVVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTM 123
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGH---TSYVSSVAFSPDGRILSSSSRDKTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737 124 QMWNYNTGECLMTFPNPDRVEISGIVHMNKVFYTTGWSK---RITNFTFQKITQALscyhwqSFHTEDILSMDKY-QNQF 199
Cdd:cd00200  118 KVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgtiKLWDLRTGKCVATL------TGHTGEVNSVAFSpDGEK 191

                        170       180       190
                 ....*....|....*....|....*....|
gi 568919737 200 LGTSSYNGDIVFWNVSTSKPILSFNASKSP 229
Cdd:cd00200  192 LLSSSSDGTIKLWDLSTGKCLGTLRGHENG 221

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 568919737 723 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 781
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 568919737  44 GLVFSRGEVLSGADNTARQRTRETQVVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTM 123
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGH---TSYVSSVAFSPDGRILSSSSRDKTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737 124 QMWNYNTGECLMTFPNPDRVEISGIVHMNKVFYTTGWSK---RITNFTFQKITQALscyhwqSFHTEDILSMDKY-QNQF 199
Cdd:cd00200  118 KVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgtiKLWDLRTGKCVATL------TGHTGEVNSVAFSpDGEK 191

                        170       180       190
                 ....*....|....*....|....*....|
gi 568919737 200 LGTSSYNGDIVFWNVSTSKPILSFNASKSP 229
Cdd:cd00200  192 LLSSSSDGTIKLWDLSTGKCLGTLRGHENG 221

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 568919737  69 VVSGCLQGLVSVWDISTG--KKRMEIPVSGIQeselTAMALDQSERCLLTGLrDGTMQMWNYNTGECLMTFpNPDRVEIS 146
Cdd:cd00200   24 LATGSGDGTIKVWDLETGelLRTLKGHTGPVR----DVAASADGTYLASGSS-DKTIRLWDLETGECVRTL-TGHTSYVS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737 147 GI--VHMNKVFYTTGWSK--RITNFTFQKITQALSCyhwqsfHTEDI--LSMDKyQNQFLGTSSYNGDIVFWNVSTSKPI 220
Cdd:cd00200   98 SVafSPDGRILSSSSRDKtiKVWDVETGKCLTTLRG------HTDWVnsVAFSP-DGTFVASSSQDGTIKLWDLRTGKCV 170

                 ....*....
gi 568919737 221 LSFNASKSP 229
Cdd:cd00200  171 ATLTGHTGE 179

WD40 repeat [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737  67 TQVVSGCLQGLVSVWDISTGKkrmEIPVSGIQESELTAMALDQSERCLLTGLRDGTMQMWNYNTGECLMTFPNPDRvEIS 146
Cdd:COG2319  217 KLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG-GVN 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737 147 GIV--HMNKVFYTTGWSKRItnftfqKI--TQALSCYHWQSFHTEDILSM----DkyqNQFLGTSSYNGDIVFWNVSTSK 218
Cdd:COG2319  293 SVAfsPDGKLLASGSDDGTV------RLwdLATGKLLRTLTGHTGAVRSVafspD---GKTLASGSDDGTVRLWDLATGE 363

                        170
                 ....*....|.
gi 568919737 219 PILSFNASKSP 229
Cdd:COG2319  364 LLRTLTGHTGA 374

WD40 repeat [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737  67 TQVVSGCLQGLVSVWDISTGKkrmEIPVSGIQESELTAMALDQSERCLLTGLRDGTMQMWNYNTGECLMTFPNPDR---- 142
Cdd:COG2319  133 KTLASGSADGTVRLWDLATGK---LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGavrs 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919737 143 VEIS--GivhmnKVFYTTGWSK--RITNFTFQKITQALscyhwqSFHTEDILSM----DkyqNQFLGTSSYNGDIVFWNV 214
Cdd:COG2319  210 VAFSpdG-----KLLASGSADGtvRLWDLATGKLLRTL------TGHSGSVRSVafspD---GRLLASGSADGTVRLWDL 275

                        170
                 ....*....|....*
gi 568919737 215 STSKPILSFNASKSP 229
Cdd:COG2319  276 ATGELLRTLTGHSGG 290

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 568919737 723 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 781
Cdd:cd21577    3 VKTDMETSFYSPSHSqlepvdlSLSKRSSPPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPP 68