N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as Krueppel-like factor 16, Basic transcription element binding protein 4/BTEB4, or Novel Sp1-like zinc finger transcription factor/2NSLP2) is a protein that in humans is encoded by the KLF16 gene. KLF16 functions as a transcription activator. It is thought to modulate dopaminergic transmission in the brain and also regulates the expression of several genes essential for metabolic and endocrine processes in sex steroid-sensitive uterine cells. KLF16 selectively binds three distinct KLF-binding sites (GC, CA, and BTE boxes). KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF16 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 KLF16.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATP-PGTPGAPPPPATAPGPGGATAAPHLLAA 80
Cdd:cd21573    1 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAPRREAAPpGTPGPPPPPPAPSPPPGGAAAAPHLLAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 144922690  81 SILADLRGGPVVAtaastAGGTSPVSSSSAASSPSSGRAPG---AAKSHR 127
Cdd:cd21573   81 SILADLRGGPGAA-----PGGASPASSSSAASSPSSGRAPGaaaAAKSHR 125

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 144922690  186 FPCPLCTKRFTRSDHLTKHARRH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as Krueppel-like factor 16, Basic transcription element binding protein 4/BTEB4, or Novel Sp1-like zinc finger transcription factor/2NSLP2) is a protein that in humans is encoded by the KLF16 gene. KLF16 functions as a transcription activator. It is thought to modulate dopaminergic transmission in the brain and also regulates the expression of several genes essential for metabolic and endocrine processes in sex steroid-sensitive uterine cells. KLF16 selectively binds three distinct KLF-binding sites (GC, CA, and BTE boxes). KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF16 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 KLF16.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATP-PGTPGAPPPPATAPGPGGATAAPHLLAA 80
Cdd:cd21573    1 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAPRREAAPpGTPGPPPPPPAPSPPPGGAAAAPHLLAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 144922690  81 SILADLRGGPVVAtaastAGGTSPVSSSSAASSPSSGRAPG---AAKSHR 127
Cdd:cd21573   81 SILADLRGGPGAA-----PGGASPASSSSAASSPSSGRAPGaaaAAKSHR 125

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 144922690  172 ELARHHRTHTGEKRFPCPLCTKRFTR 197
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690 158 CDWPGCDKKFARSDELARHHRT--HTGE--KRFPCP--LCTKRFTRSDHLTKHARRHPG--FRPELLRRPGARSVSPSDS 229
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSisPAKEKLLNSSSKFSPLLNN 369

                 ..
gi 144922690 230 LP 231
Cdd:COG5048  370 EP 371

N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as Krueppel-like factor 16, Basic transcription element binding protein 4/BTEB4, or Novel Sp1-like zinc finger transcription factor/2NSLP2) is a protein that in humans is encoded by the KLF16 gene. KLF16 functions as a transcription activator. It is thought to modulate dopaminergic transmission in the brain and also regulates the expression of several genes essential for metabolic and endocrine processes in sex steroid-sensitive uterine cells. KLF16 selectively binds three distinct KLF-binding sites (GC, CA, and BTE boxes). KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF16 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 KLF16.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATP-PGTPGAPPPPATAPGPGGATAAPHLLAA 80
Cdd:cd21573    1 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAPRREAAPpGTPGPPPPPPAPSPPPGGAAAAPHLLAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 144922690  81 SILADLRGGPVVAtaastAGGTSPVSSSSAASSPSSGRAPG---AAKSHR 127
Cdd:cd21573   81 SILADLRGGPGAA-----PGGASPASSSSAASSPSSGRAPGaaaAAKSHR 125

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 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 KLF14.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREAT------PPGTPGAPPPPATAPGPGGATAAP 75
Cdd:cd21576    1 SAAVACLDYFAAECLVSMSAGAVLHRRAPDPEGAGGAAGSEVGAAPPESAlpgpgpPGPAWVPPLLQVPAPSPGAGGAAP 80

                         90
                 ....*....|....
gi 144922690  76 HLLAASILADLRGG 89
Cdd:cd21576   81 HLLAASVLADLRGG 94

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690 124 KSHRCPfhGCAKAYYKSSHLKSHLRT--HTGE--RPFACDWPGCDKKFARSDELARHHRTHTGEKRFPCPL--CTKRFTR 197
Cdd:COG5048  288 LPIKSK--QCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSP 365

                         90
                 ....*....|..
gi 144922690 198 SDHLTKHARRHP 209
Cdd:COG5048  366 LLNNEPPQSLQQ 377

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 144922690  172 ELARHHRTHTGEKRFPCPLCTKRFTR 197
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 144922690  142 HLKSHLRTHTGERPFACdwPGCDKKFAR 169
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26

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 144922690  186 FPCPLCTKRFTRSDHLTKHARRH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 144922690 154 RPFACdwPGCDKKFARSDELARHHRTHTGEKRFPC--PLCTKRFTRSDHLTKHARRHP 209
Cdd:COG5048   32 RPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHH 87