N-terminal domain of Kruppel-like factor 13; Kruppel-like factor 13 (KLF13; also known as Krueppel-like factor 13, RANTES factor of late activated T lymphocytes 1/RFLAT-1, or Fetal Kruppel-like factor-2/FKLF-2), is a protein that in humans is encoded by the KLF13 gene. It was originally cloned from fetal globin-expressing tissues, though it has also been cloned from bone marrow, striated muscles, and a subset of T cells where it is highly expressed. KLF13 plays a role in heart development and morphogenesis and is thought to play a role in obesity. It regulates the expression of the chemokine RANTES in T lymphocytes and has been shown to interact with CREB-binding protein, heat shock protein 47, and PCAF. 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. KLF13 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 KLF13.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995   7 VDHFAAECLVSMSSRAVVHGPREGPESRPEGAAvaaTPTLPRVEERRDGKDSASLFVVARILADLNQQAPAPAPAERREG 86
Cdd:cd21571   1 VDHFAAECLVSMSSRAIVHGPKGNPEPKPASEA---APPPENGEDRREGKDNSSLFVVARILADLNQQVPKPSAEQEKSN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995  87 AAARKARTPCRLPPpapeptspgaegaaaappspawSEPEPEAGLEPeREPGPAGSGEPGLRQRVRRGRSRADLESPQRK 166
Cdd:cd21571  78 ESAPREGEEPPLPA----------------------GKGGDGSAATP-TSPGGAAAAPPTPKQRSRRGRGRSDPESPQKK 134

                ..
gi 37693995 167 HK 168
Cdd:cd21571 135 HK 136

N-terminal domain of Kruppel-like factor 13; Kruppel-like factor 13 (KLF13; also known as Krueppel-like factor 13, RANTES factor of late activated T lymphocytes 1/RFLAT-1, or Fetal Kruppel-like factor-2/FKLF-2), is a protein that in humans is encoded by the KLF13 gene. It was originally cloned from fetal globin-expressing tissues, though it has also been cloned from bone marrow, striated muscles, and a subset of T cells where it is highly expressed. KLF13 plays a role in heart development and morphogenesis and is thought to play a role in obesity. It regulates the expression of the chemokine RANTES in T lymphocytes and has been shown to interact with CREB-binding protein, heat shock protein 47, and PCAF. 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. KLF13 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 KLF13.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995   7 VDHFAAECLVSMSSRAVVHGPREGPESRPEGAAvaaTPTLPRVEERRDGKDSASLFVVARILADLNQQAPAPAPAERREG 86
Cdd:cd21571   1 VDHFAAECLVSMSSRAIVHGPKGNPEPKPASEA---APPPENGEDRREGKDNSSLFVVARILADLNQQVPKPSAEQEKSN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995  87 AAARKARTPCRLPPpapeptspgaegaaaappspawSEPEPEAGLEPeREPGPAGSGEPGLRQRVRRGRSRADLESPQRK 166
Cdd:cd21571  78 ESAPREGEEPPLPA----------------------GKGGDGSAATP-TSPGGAAAAPPTPKQRSRRGRGRSDPESPQKK 134

                ..
gi 37693995 167 HK 168
Cdd:cd21571 135 HK 136

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 37693995   227 FSCPICEKRFMRSDHLTKHARRH 249
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

N-terminal domain of Kruppel-like factor 13; Kruppel-like factor 13 (KLF13; also known as Krueppel-like factor 13, RANTES factor of late activated T lymphocytes 1/RFLAT-1, or Fetal Kruppel-like factor-2/FKLF-2), is a protein that in humans is encoded by the KLF13 gene. It was originally cloned from fetal globin-expressing tissues, though it has also been cloned from bone marrow, striated muscles, and a subset of T cells where it is highly expressed. KLF13 plays a role in heart development and morphogenesis and is thought to play a role in obesity. It regulates the expression of the chemokine RANTES in T lymphocytes and has been shown to interact with CREB-binding protein, heat shock protein 47, and PCAF. 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. KLF13 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 KLF13.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995   7 VDHFAAECLVSMSSRAVVHGPREGPESRPEGAAvaaTPTLPRVEERRDGKDSASLFVVARILADLNQQAPAPAPAERREG 86
Cdd:cd21571   1 VDHFAAECLVSMSSRAIVHGPKGNPEPKPASEA---APPPENGEDRREGKDNSSLFVVARILADLNQQVPKPSAEQEKSN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995  87 AAARKARTPCRLPPpapeptspgaegaaaappspawSEPEPEAGLEPeREPGPAGSGEPGLRQRVRRGRSRADLESPQRK 166
Cdd:cd21571  78 ESAPREGEEPPLPA----------------------GKGGDGSAATP-TSPGGAAAAPPTPKQRSRRGRGRSDPESPQKK 134

                ..
gi 37693995 167 HK 168
Cdd:cd21571 135 HK 136

N-terminal domain of Kruppel-like factor 9; Kruppel-like factor 9 (KLF9; also known as Krueppel-like factor 9, or Basic Transcription Element Binding Protein 1/BTEB Protein 1) is a protein that in humans is encoded by the KLF9 gene. KLF9 is critical for the inhibition of growth and development of tumors. It is involved in cell differentiation of B cells, keratinocytes, and neurons. It is also a key transcriptional regulator for uterine endometrial cell proliferation, adhesion, and differentiation; these are processes essential for pregnancy success and are subverted during tumorigenesis. 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. KLF9 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 KLF9.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995   3 AAAYVDHFAAECLVSMSSRAVVHGPREGPESRPEgaAVAATPTLPRVEERRD-GKDSASLFVVARILADLNQQAPAPAPA 81
Cdd:cd21578   1 AVAYMDFVAAQCLVSISNRAAVPEHGRAPEPPEQ--RLPEREVTKEHGDPGDaWKDYCTLLTIAKSLLDLNKYRPLPSPS 78

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
                ....*....|....*....|....*....|....*....|....*
gi 37693995   2 AAAAYVDHFAAECLVSMSSRAVVHGPREGPE--SRPEGAAVAATP 44
Cdd:cd21576   2 AAVACLDYFAAECLVSMSAGAVLHRRAPDPEgaGGAAGSEVGAAP 46

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995 199 CSWQDCNKKFARSDELARHYRT--HTGE--KKFSCPI--CEKRFMRSDHLTKHARRH--ANFHPGMLQRRG-------GG 263
Cdd:COG5048 290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHtsISPAKEKLLNSSskfspllNN 369

                        90       100
                ....*....|....*....|....
gi 37693995 264 SRTGSLSDYSRSDASSPTISPASS 287
Cdd:COG5048 370 EPPQSLQQYKDLKNDKKSETLSNS 393

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37693995 162 SPQRKHKCHYAGCEKVYGKSSHLKAHLRTHTGERPFACSWQDCNKKFARSDELARHYRTHTgEKKFSCPICEKRFMRSDH 241
Cdd:COG5048 382 KNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLD 460

                ....
gi 37693995 242 LTKH 245
Cdd:COG5048 461 LSNH 464

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 37693995   183 HLKAHLRTHTGERPFACswQDCNKKFAR 210
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 37693995   197 FACSwqDCNKKFARSDELARHYRTH 221
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23