N-terminal domain of Kruppel-like factor (KLF) 6, KLF7, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 6, KLF7, and similar proteins, including KLF Luna, a Drosophila KLF6/KLF7. KLF6 contributes to cell proliferation, differentiation, cell death and signal transduction. Hepatocyte expression of KLF6 regulates hepatic fatty acid and glucose metabolism via transcriptional activation of liver glucokinase and post-transcriptional regulation of the nuclear receptor peroxisome proliferator activated receptor alpha (PPARa). KLF7 is involved in regulation of the development and function of the nervous system and adipose tissue, type 2 diabetes, blood diseases, as well as pluripotent cell maintenance. KLF Luna is maternally required for synchronized nuclear and centrosome cycles in the preblastoderm embryo. KLF6 and KLF7 are transcriptional activators. They belong 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 related N-terminal domains of KLF6, KLF7, and similar proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45580796   2 DILPSGNIFSELERICTTGYYSSQPSIEDQWQQTCYELERYLRDEPKLQKKMHSNLDNPWD--IFSTPARLLEELKIKEQ 79
Cdd:cd21973   1 DILPSGNIFRELQVVHDTGYFSAQPSLEDHWQQTCYEMERYLKDEPKLTSYKKDPSDSPWSpwDLFTPPSEESESSDSDL 80

                ...
gi 45580796  80 HLD 82
Cdd:cd21973  81 SLL 83

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45580796 455 SQRSEKSANGSSKPHHPRQHHSDH-SPDAKRRIHKCQFLGCKKVYTKSSHLKAHQRT--HTGE--KPYKCSWEGCEWRFA 529
Cdd:COG5048 255 SSASESPRSSLPTASSQSSSPNESdSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFS 334

                        90       100       110
                ....*....|....*....|....*....|
gi 45580796 530 RSDELTRHYRKHTGAKPFKCRNCDRCFSRS 559
Cdd:COG5048 335 RNDALKRHILLHTSISPAKEKLLNSSSKFS 364

N-terminal domain of Kruppel-like factor (KLF) 6, KLF7, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 6, KLF7, and similar proteins, including KLF Luna, a Drosophila KLF6/KLF7. KLF6 contributes to cell proliferation, differentiation, cell death and signal transduction. Hepatocyte expression of KLF6 regulates hepatic fatty acid and glucose metabolism via transcriptional activation of liver glucokinase and post-transcriptional regulation of the nuclear receptor peroxisome proliferator activated receptor alpha (PPARa). KLF7 is involved in regulation of the development and function of the nervous system and adipose tissue, type 2 diabetes, blood diseases, as well as pluripotent cell maintenance. KLF Luna is maternally required for synchronized nuclear and centrosome cycles in the preblastoderm embryo. KLF6 and KLF7 are transcriptional activators. They belong 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 related N-terminal domains of KLF6, KLF7, and similar proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45580796   2 DILPSGNIFSELERICTTGYYSSQPSIEDQWQQTCYELERYLRDEPKLQKKMHSNLDNPWD--IFSTPARLLEELKIKEQ 79
Cdd:cd21973   1 DILPSGNIFRELQVVHDTGYFSAQPSLEDHWQQTCYEMERYLKDEPKLTSYKKDPSDSPWSpwDLFTPPSEESESSDSDL 80

                ...
gi 45580796  80 HLD 82
Cdd:cd21973  81 SLL 83

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45580796 455 SQRSEKSANGSSKPHHPRQHHSDH-SPDAKRRIHKCQFLGCKKVYTKSSHLKAHQRT--HTGE--KPYKCSWEGCEWRFA 529
Cdd:COG5048 255 SSASESPRSSLPTASSQSSSPNESdSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFS 334

                        90       100       110
                ....*....|....*....|....*....|
gi 45580796 530 RSDELTRHYRKHTGAKPFKCRNCDRCFSRS 559
Cdd:COG5048 335 RNDALKRHILLHTSISPAKEKLLNSSSKFS 364

N-terminal domain of Kruppel-like factor (KLF) 6, KLF7, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 6, KLF7, and similar proteins, including KLF Luna, a Drosophila KLF6/KLF7. KLF6 contributes to cell proliferation, differentiation, cell death and signal transduction. Hepatocyte expression of KLF6 regulates hepatic fatty acid and glucose metabolism via transcriptional activation of liver glucokinase and post-transcriptional regulation of the nuclear receptor peroxisome proliferator activated receptor alpha (PPARa). KLF7 is involved in regulation of the development and function of the nervous system and adipose tissue, type 2 diabetes, blood diseases, as well as pluripotent cell maintenance. KLF Luna is maternally required for synchronized nuclear and centrosome cycles in the preblastoderm embryo. KLF6 and KLF7 are transcriptional activators. They belong 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 related N-terminal domains of KLF6, KLF7, and similar proteins.

                        10        20        30
                ....*....|....*....|....*....|..
gi 45580796 457 RSEKSANGSSKPHHPRQHHSDHSPDAKRRIHK 488
Cdd:cd21973 107 WTPPSSPESSRSHPSSSYTKSSSPDSKRRIHK 138

N-terminal domain of Kruppel-like factor (KLF) 6, KLF7, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 6, KLF7, and similar proteins, including KLF Luna, a Drosophila KLF6/KLF7. KLF6 contributes to cell proliferation, differentiation, cell death and signal transduction. Hepatocyte expression of KLF6 regulates hepatic fatty acid and glucose metabolism via transcriptional activation of liver glucokinase and post-transcriptional regulation of the nuclear receptor peroxisome proliferator activated receptor alpha (PPARa). KLF7 is involved in regulation of the development and function of the nervous system and adipose tissue, type 2 diabetes, blood diseases, as well as pluripotent cell maintenance. KLF Luna is maternally required for synchronized nuclear and centrosome cycles in the preblastoderm embryo. KLF6 and KLF7 are transcriptional activators. They belong 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 related N-terminal domains of KLF6, KLF7, and similar proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45580796   2 DILPSGNIFSELERICTTGYYSSQPSIEDQWQQTCYELERYLRDEPKLQKKMHSNLDNPWD--IFSTPARLLEELKIKEQ 79
Cdd:cd21973   1 DILPSGNIFRELQVVHDTGYFSAQPSLEDHWQQTCYEMERYLKDEPKLTSYKKDPSDSPWSpwDLFTPPSEESESSDSDL 80

                ...
gi 45580796  80 HLD 82
Cdd:cd21973  81 SLL 83

N-terminal domain of Kruppel-like factor 6; Kruppel-like factor 6 (KLF6; also known as Krueppel-like factor 6, BCD1, CBA1, COPEB, CPBP, GBF, PAC1, ST12, or ZF9) is a protein that, in humans, is encoded by the KLF6 gene. KLF6 contributes to cell proliferation, differentiation, cell death, and signal transduction. Hepatocyte expression of KLF6 regulates hepatic fatty acid and glucose metabolism via transcriptional activation of liver glucokinase and post-transcriptional regulation of the nuclear receptor peroxisome proliferator activated receptor alpha (PPARa). KLF6-expression contributes to hepatic insulin resistance and the progression of non-alcoholic fatty liver disease (NAFLD) to non-alcoholic steatohepatitis (NASH) and NASH-cirrhosis. KLF6 also affects peroxisome proliferator activated receptor gamma (PPARgamma)-signaling in NAFLD. KLF6 has also been identified as a tumor suppressor gene that is inactivated or downregulated in different cancers, including prostate, colon, and hepatocellular carcinomas. KLF6 transactivates genes controlling cell proliferation, including p21, E-cadherin, and pituary tumor-transforming gene 1 (PTTG1). KLF6 functions as a transcriptional activator. It 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 KLF6.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 45580796   2 DILPSGNIFSELERICTTGYYSSQPSIEDQWQQTCYELERYLRDEP 47
Cdd:cd21586   1 DVIPMCSIFQELQIVHDTGYFSALPSLEEYWQQTCLELERYLQSEP 46

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 45580796   547 FKCRNCDRCFSRSDHLALHMKRH 569
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 45580796   503 HLKAHQRTHTGEKPYKCswEGCEWRFAR 530
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 45580796   487 HKCQflGCKKVYTKSSHLKAHQRTH 511
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23