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 4557375    3 AAAYMDFVAAQCLVSISNRAAVPEHGVAPDAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVC 82
Cdd:cd21578   1 AVAYMDFVAAQCLVSISNRAAVPEHGRAPEPPEQRLPEREVTKEHGDPGDAWKDYCTLLTIAKSLLDLNKYRPLPSPSVC 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557375   83 SDSLESPDEDMGSDSDVTTESGSSPSHSPEERQDPGSAPSPLSLLHPGVAAKGKHASEKRHK 144
Cdd:cd21578  81 SDSLESPDEDLGSDSDVTTESGSSPSHSPEERSDSGSPPSPLSLLHPGVAAKGKLASEKRHK 142

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 4557375    3 AAAYMDFVAAQCLVSISNRAAVPEHGVAPDAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVC 82
Cdd:cd21578   1 AVAYMDFVAAQCLVSISNRAAVPEHGRAPEPPEQRLPEREVTKEHGDPGDAWKDYCTLLTIAKSLLDLNKYRPLPSPSVC 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557375   83 SDSLESPDEDMGSDSDVTTESGSSPSHSPEERQDPGSAPSPLSLLHPGVAAKGKHASEKRHK 144
Cdd:cd21578  81 SDSLESPDEDLGSDSDVTTESGSSPSHSPEERSDSGSPPSPLSLLHPGVAAKGKLASEKRHK 142

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 4557375    189 ELTRHYRTHTGEKQFRCPLCEKRF 212
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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 4557375    3 AAAYMDFVAAQCLVSISNRAAVPEHGVAPDAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVC 82
Cdd:cd21578   1 AVAYMDFVAAQCLVSISNRAAVPEHGRAPEPPEQRLPEREVTKEHGDPGDAWKDYCTLLTIAKSLLDLNKYRPLPSPSVC 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557375   83 SDSLESPDEDMGSDSDVTTESGSSPSHSPEERQDPGSAPSPLSLLHPGVAAKGKHASEKRHK 144
Cdd:cd21578  81 SDSLESPDEDLGSDSDVTTESGSSPSHSPEERSDSGSPPSPLSLLHPGVAAKGKLASEKRHK 142

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 4557375    7 MDFVAAQCLVSISNRAAVpeHGVAPDAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKyrpiQTPSVCSDSL 86
Cdd:cd21571   1 VDHFAAECLVSMSSRAIV--HGPKGNPEPKPASEAAPPPENGEDRREGKDNSSLFVVARILADLNQ----QVPKPSAEQE 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557375   87 ESPDE--DMGSDSDVTTESGSSPSHSPEERQDPGSAPSPLSLLHpGVAAKGKHASE---KRHK 144
Cdd:cd21571  75 KSNESapREGEEPPLPAGKGGDGSAATPTSPGGAAAAPPTPKQR-SRRGRGRSDPEspqKKHK 136

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557375   79 PSVCSDSLESPDEDmGSDSDVTTESGSSPSHSPEERQDpgsapSPLSLLHPGVAAKGKhaSEKRHKCPYSGCGKVYGKSS 158
Cdd:COG5189 294 KSVGNKEIRGGIST-GEMIDVRKLPCTNSSSNGKLAHG-----GERNIDTPSRMLKVK--DGKPYKCPVEGCNKKYKNQN 365

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557375  159 HLKAHYRV-HTGERPFPCTWPDCLKKFSRSDeltrhyrthtgeKQFRCPLCEKRFMRSDHLTKHaRRHT 226
Cdd:COG5189 366 GLKYHMLHgHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLKYH-RKHS 421

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 4557375    203 FRCPLCEKRFMRSDHLTKHARRH 225
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

hypothetical protein

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4557375   172 PFPCtwPDCLKKFSRSDELTRH--YRTHTgekqFRCPLCEKRFMRSDHLTKH 221
Cdd:PHA00733  73 PYVC--PLCLMPFSSSVSLKQHirYTEHS----KVCPVCGKEFRNTDSTLDH 118

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 4557375    159 HLKAHYRVHTGERPFPCtwPDCLKKFSR 186
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26