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 1720396571  381 HPNWCQQVKYIPQLNVVASCSAVEKsslvlIILPGKEPEKPRLSSLNLRKGILCFDYCPDRNFLATGGYDPHIRLWNpLV 460
Cdd:cd00200      8 HTGGVTCVAFSPDGKLLATGSGDGT-----IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-LE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  461 SKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTLicstyn 540
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNSVAFSPDGTF------ 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720396571  541 VVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTMQMWNYNTGECLMTF 609
Cdd:cd00200    150 VASSSQDGTIKLWDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215

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 1720396571 1195 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 1253
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 1720396571  381 HPNWCQQVKYIPQLNVVASCSAVEKsslvlIILPGKEPEKPRLSSLNLRKGILCFDYCPDRNFLATGGYDPHIRLWNpLV 460
Cdd:cd00200      8 HTGGVTCVAFSPDGKLLATGSGDGT-----IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-LE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  461 SKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTLicstyn 540
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNSVAFSPDGTF------ 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720396571  541 VVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTMQMWNYNTGECLMTF 609
Cdd:cd00200    150 VASSSQDGTIKLWDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215

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 1720396571   461 SKKPVWLMKGHQTSVTHLLVNSrNASILISISRDKNIRVWD 501
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40

EF-hand domain pair;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720396571  126 ENGALKKEGFIRIMK-GVLSSMSEEMLELLFLKVDSDCNGFVTWQKYVDYMMRE 178
Cdd:pfam13833    1 EKGVITREELKRALAlLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54

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 1720396571 1195 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 1253
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 1720396571  381 HPNWCQQVKYIPQLNVVASCSAVEKsslvlIILPGKEPEKPRLSSLNLRKGILCFDYCPDRNFLATGGYDPHIRLWNpLV 460
Cdd:cd00200      8 HTGGVTCVAFSPDGKLLATGSGDGT-----IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-LE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  461 SKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGKlfplgNCPITSTYFYRSSTLicstyn 540
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNSVAFSPDGTF------ 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720396571  541 VVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTMQMWNYNTGECLMTF 609
Cdd:cd00200    150 VASSSQDGTIKLWDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  439 PDRNFLATGGYDPHIRLWNpLVSKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGklfpl 518
Cdd:COG2319    130 PDGKTLASGSADGTVRLWD-LATGKLLRTLTGHSGAVTSVAF-SPDGKLLASGSDDGTVRLWDLATGKLLRTLTG----- 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  519 GNCPITSTYFYRSSTLIcstynvVSGCLQGLVSVWDISTGKkrmEIPVSGIQESELTAMALDQSERCLLTGLRDGTMQMW 598
Cdd:COG2319    203 HTGAVRSVAFSPDGKLL------ASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  599 NYNTGECLMTFPNPDRvEISGIV--HMNKVFYTTGWSKRItnftfqKI--TQALSCYHWQSFHTEDILSM----DkyqNQ 670
Cdd:COG2319    274 DLATGELLRTLTGHSG-GVNSVAfsPDGKLLASGSDDGTV------RLwdLATGKLLRTLTGHTGAVRSVafspD---GK 343

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1720396571  671 FLGTSSYNGDIVFWNVSTSKPILSFNASKSP 701
Cdd:COG2319    344 TLASGSDDGTVRLWDLATGELLRTLTGHTGA 374

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  439 PDRNFLATGGYDPHIRLWNpLVSKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGklfpl 518
Cdd:COG2319     88 PDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGAVRSVAF-SPDGKTLASGSADGTVRLWDLATGKLLRTLTG----- 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  519 GNCPITSTYFYRSSTLIcstynvVSGCLQGLVSVWDISTGKKRMEIPVSgiqESELTAMALDQSERCLLTGLRDGTMQMW 598
Cdd:COG2319    161 HSGAVTSVAFSPDGKLL------ASGSDDGTVRLWDLATGKLLRTLTGH---TGAVRSVAFSPDGKLLASGSADGTVRLW 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  599 NYNTGECLMTFPNPDR----VEIS--GivhmnKVFYTTGWSKRItnftfqKI--TQALSCYHWQSFHTEDILSM----Dk 666
Cdd:COG2319    232 DLATGKLLRTLTGHSGsvrsVAFSpdG-----RLLASGSADGTV------RLwdLATGELLRTLTGHSGGVNSVafspD- 299

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1720396571  667 yqNQFLGTSSYNGDIVFWNVSTSKPILSFNASKSP 701
Cdd:COG2319    300 --GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGA 332

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 1720396571  469 KGHQTSVTHLLVNSRNaSILISISRDKNIRVWDLQDYVCLQSFCGKLFPLGNCpitstyfyrssTLICSTYNVVSGCLQG 548
Cdd:cd00200      6 KGHTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDV-----------AASADGTYLASGSSDK 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  549 LVSVWDISTGKKRMEIpvSGiQESELTAMALDQSERCLLTGLRDGTMQMWNYNTGECLMTFPNPDRVEISGIVHMNKVFY 628
Cdd:cd00200     74 TIRLWDLETGECVRTL--TG-HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFV 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720396571  629 TTGWSK---RITNFTFQKITQALscyhwqSFHTEDILSMDKY-QNQFLGTSSYNGDIVFWNVSTSKPILSFNASKSP 701
Cdd:cd00200    151 ASSSQDgtiKLWDLRTGKCVATL------TGHTGEVNSVAFSpDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG 221

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  439 PDRNFLATGGYDPHIRLWNpLVSKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWDLQDYVCLQSFCGklfpl 518
Cdd:COG2319    298 PDGKLLASGSDDGTVRLWD-LATGKLLRTLTGHTGAVRSVAF-SPDGKTLASGSDDGTVRLWDLATGELLRTLTG----- 370

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720396571  519 GNCPITSTYFYRSSTLIcstynvVSGCLQGLVSVWDIST 557
Cdd:COG2319    371 HTGAVTSVAFSPDGRTL------ASGSADGTVRLWDLAT 403

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 1720396571  205 HGSEVVKVACLTKRfkkmGRFLTVTKDGILQFWS-ETFSMLESFHlsqskqyGHQQmWVIDVAYLHNMSLIAVASTELKI 283
Cdd:cd00200     50 HTGPVRDVAASADG----TYLASGSSDKTIRLWDlETGECVRTLT-------GHTS-YVSSVAFSPDGRILSSSSRDKTI 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  284 EFFDIGGYKCIRAFTvidldscvmvmdywtdCHKAVfcygdtkGNATIFISDN--VAGglfnpqilpraSKWDH----WF 357
Cdd:cd00200    118 KVWDVETGKCLTTLR----------------GHTDW-------VNSVAFSPDGtfVAS-----------SSQDGtiklWD 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  358 TVSLKkllnekapLYRSFRMkglHPNWCQQVKYIPQLNVVASCSA------VEKSSLVLI-ILPGKEpekprlsslnlrK 430
Cdd:cd00200    164 LRTGK--------CVATLTG---HTGEVNSVAFSPDGEKLLSSSSdgtiklWDLSTGKCLgTLRGHE------------N 220

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720396571  431 GILCFDYCPDRNFLATGGYDPHIRLWNpLVSKKPVWLMKGHQTSVTHLLVnSRNASILISISRDKNIRVWD 501
Cdd:cd00200    221 GVNSVAFSPDGYLLASGSEDGTIRVWD-LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289

coronin; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720396571  447 GGYDPHIRLWNPlVSKKPVWLMKGHQTSVTHLLVNSRNASILISISRDKNIRVWDL----------QDYVC-LQSFCGKL 515
Cdd:PTZ00420    50 GGLIGAIRLENQ-MRKPPVIKLKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIphndesvkeiKDPQCiLKGHKKKI 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720396571  516 FPLGNCPItsTYFyrsstLICSTynvvsgCLQGLVSVWDISTGKKRMEI 564
Cdd:PTZ00420   129 SIIDWNPM--NYY-----IMCSS------GFDSFVNIWDIENEKRAFQI 164

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

                            10        20
                    ....*....|....*....|....*....
gi 1720396571   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 1720396571 1195 IPTDMVAGSPAATPS-------SLSMVSVGQSPSNWSTSLKPLSSTSFLRPSSASPAHSGSSTPPH 1253
Cdd:cd21577      3 VKTDMETSFYSPSHSqlepvdlSLSKRSSPPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPP 68