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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801  49 TPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPShrrASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPvMAA 128
Cdd:cd21577    9 TSFYSPSHSQLEPVDLSLSKRSSPPSSSSSSSSSSSSS---SSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLPP-PVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801 129 ALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDN----SNSGMPVPVIESYEKPLLQKKIKIEPGIEP 204
Cdd:cd21577   85 PPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQPIMVSSSPPPDDdhhhHKASSMKPSELGGDNHELHKPIKTEPRPEH 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568933801 205 QRtDYYPEEMSPPLMNPVSPPQallqENHPSVIVQPGKRPLPVESPDTQRKRRIH 259
Cdd:cd21577  165 AQ-DPYSEEMSSSVISSPPEYE----SNTPSVIVHPGKRPLPVESPDTLKKRRIH 214

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|....*
gi 568933801  259 HRCDYdgCNKVYTKSSHLKAHRRTH 283
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801  49 TPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPShrrASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPvMAA 128
Cdd:cd21577    9 TSFYSPSHSQLEPVDLSLSKRSSPPSSSSSSSSSSSSS---SSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLPP-PVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801 129 ALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDN----SNSGMPVPVIESYEKPLLQKKIKIEPGIEP 204
Cdd:cd21577   85 PPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQPIMVSSSPPPDDdhhhHKASSMKPSELGGDNHELHKPIKTEPRPEH 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568933801 205 QRtDYYPEEMSPPLMNPVSPPQallqENHPSVIVQPGKRPLPVESPDTQRKRRIH 259
Cdd:cd21577  165 AQ-DPYSEEMSSSVISSPPEYE----SNTPSVIVHPGKRPLPVESPDTLKKRRIH 214

FOG: Zn-finger [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801 169 SEEMDNSNSGMPVPVIESYEKPLLQKKIKIEPGIEPQRTDYYPEEMSPPLMNPVSPPQALLQ----------------EN 232
Cdd:COG5048  182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQspsslsssdssssaseSP 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801 233 HPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRT--HTGE--KPYKCTWEGCTWKFARSDELTR 308
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKR 341

                        170       180
                 ....*....|....*....|...
gi 568933801 309 HFRKHTGIKPFQCPDCDRSFSRS 331
Cdd:COG5048  342 HILLHTSISPAKEKLLNSSSKFS 364

Zinc-finger double domain;

                          10
                  ....*....|....*...
gi 568933801  275 HLKAHRRTHTGEKPYKCT 292
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP 18

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801  49 TPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPShrrASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPvMAA 128
Cdd:cd21577    9 TSFYSPSHSQLEPVDLSLSKRSSPPSSSSSSSSSSSSS---SSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLPP-PVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933801 129 ALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDN----SNSGMPVPVIESYEKPLLQKKIKIEPGIEP 204
Cdd:cd21577   85 PPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQPIMVSSSPPPDDdhhhHKASSMKPSELGGDNHELHKPIKTEPRPEH 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568933801 205 QRtDYYPEEMSPPLMNPVSPPQallqENHPSVIVQPGKRPLPVESPDTQRKRRIH 259
Cdd:cd21577  165 AQ-DPYSEEMSSSVISSPPEYE----SNTPSVIVHPGKRPLPVESPDTLKKRRIH 214

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 568933801  319 FQCPDCDRSFSRSDHLALHRKRH 341
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|....*
gi 568933801  259 HRCDYdgCNKVYTKSSHLKAHRRTH 283
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10
                  ....*....|....*...
gi 568933801  275 HLKAHRRTHTGEKPYKCT 292
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP 18

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                          10        20
                  ....*....|....*....|...
gi 568933801  319 FQCPDCDRSFSRSDHLALHRKRH 341
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23