N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 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 KLF11.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161  23 LEQTDMEAVEALVCMSSWGQRSQKGDLLRIRPLTPVSDSGDVTttvHMDAATPELPKDFHSLSTLCITPPQSPDLVEPST 102
Cdd:cd21584    1 LEQNDLEAVEALVCMSSWGQRSQKGDLLKIRPLTPASDSCDSL---TLHPAAPELPKDFHSLSSLCMTPPHSPSFAEPST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 103 RTPvspqvtdskactatdvlqssavvaralsggaergllglepvpSSPCRAKGTSVIRHTGESPAacfptiqtpdcrlsd 182
Cdd:cd21584   78 TAP------------------------------------------PPPCRAMATSVIRHTADSSP--------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 183 sregeeqllghfetlqdthltdsllstnlvscqpclhksggllltdkgqqagwpgavqtcspknyendlprkttpliSVS 262
Cdd:cd21584  101 -----------------------------------------------------------------------------PVP 103

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 263 VPAPPVLCQMIPVTGQSSMLPAFLKPPPqLSVGTVRPILAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANVM 342
Cdd:cd21584  104 VPSPPVLCQMIPVSGQSGMISAFLQPPA-LSAGTVKPILPQTAPASQPLLVGSPVPQGTVMLVLPQASVPQPPQCPQTVM 182

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 295148161 343 AAGNTKLLPLAPAPVFITSSQNCVPQVDFSRRRNY 377
Cdd:cd21584  183 TLGNTKLLPLAPAPVFIPSGQSCAPQVDFSRRRNY 217

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 295148161  437 FVCPVCDRRFMRSDHLTKHARRH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 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 KLF11.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161  23 LEQTDMEAVEALVCMSSWGQRSQKGDLLRIRPLTPVSDSGDVTttvHMDAATPELPKDFHSLSTLCITPPQSPDLVEPST 102
Cdd:cd21584    1 LEQNDLEAVEALVCMSSWGQRSQKGDLLKIRPLTPASDSCDSL---TLHPAAPELPKDFHSLSSLCMTPPHSPSFAEPST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 103 RTPvspqvtdskactatdvlqssavvaralsggaergllglepvpSSPCRAKGTSVIRHTGESPAacfptiqtpdcrlsd 182
Cdd:cd21584   78 TAP------------------------------------------PPPCRAMATSVIRHTADSSP--------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 183 sregeeqllghfetlqdthltdsllstnlvscqpclhksggllltdkgqqagwpgavqtcspknyendlprkttpliSVS 262
Cdd:cd21584  101 -----------------------------------------------------------------------------PVP 103

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 263 VPAPPVLCQMIPVTGQSSMLPAFLKPPPqLSVGTVRPILAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANVM 342
Cdd:cd21584  104 VPSPPVLCQMIPVSGQSGMISAFLQPPA-LSAGTVKPILPQTAPASQPLLVGSPVPQGTVMLVLPQASVPQPPQCPQTVM 182

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 295148161 343 AAGNTKLLPLAPAPVFITSSQNCVPQVDFSRRRNY 377
Cdd:cd21584  183 TLGNTKLLPLAPAPVFIPSGQSCAPQVDFSRRRNY 217

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 295148161  393 HLKAHLRTHTGEKPFNCswDGCDKKFAR 420
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 295148161   437 FVCPVCDRRFMRSDHLTKHARRH 459
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 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 KLF11.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161  23 LEQTDMEAVEALVCMSSWGQRSQKGDLLRIRPLTPVSDSGDVTttvHMDAATPELPKDFHSLSTLCITPPQSPDLVEPST 102
Cdd:cd21584    1 LEQNDLEAVEALVCMSSWGQRSQKGDLLKIRPLTPASDSCDSL---TLHPAAPELPKDFHSLSSLCMTPPHSPSFAEPST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 103 RTPvspqvtdskactatdvlqssavvaralsggaergllglepvpSSPCRAKGTSVIRHTGESPAacfptiqtpdcrlsd 182
Cdd:cd21584   78 TAP------------------------------------------PPPCRAMATSVIRHTADSSP--------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 183 sregeeqllghfetlqdthltdsllstnlvscqpclhksggllltdkgqqagwpgavqtcspknyendlprkttpliSVS 262
Cdd:cd21584  101 -----------------------------------------------------------------------------PVP 103

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 263 VPAPPVLCQMIPVTGQSSMLPAFLKPPPqLSVGTVRPILAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANVM 342
Cdd:cd21584  104 VPSPPVLCQMIPVSGQSGMISAFLQPPA-LSAGTVKPILPQTAPASQPLLVGSPVPQGTVMLVLPQASVPQPPQCPQTVM 182

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 295148161 343 AAGNTKLLPLAPAPVFITSSQNCVPQVDFSRRRNY 377
Cdd:cd21584  183 TLGNTKLLPLAPAPVFIPSGQSCAPQVDFSRRRNY 217

N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as Krueppel-like factor 10; early growth response(EGR)-alpha/EGRA; TGFbeta inducible early gene-1/TIEG1) is a protein that in humans is encoded by the KLF10 gene. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. It may also play a role in adipocyte differentiation and adipose tissue function. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10 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 KLF10.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161  23 LEQTDMEAVEALVCMSS-WGQRSQKgdLLRIRPLTPVSDSGDvtttvhmDAATPeLPKDFHSLSTLCITPPQSPDLVEPS 101
Cdd:cd21572    1 MGAGDMEAVEALMSMTKhWKTRSFR--LRHFRPLTPSSDSSE-------DDDLP-SPADFHDSPPFCMTPPYSPPHFEAT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 102 TRTPVSPQVTDSKACTATDVLQSsavvaralsggaergllglePVPSSPCRAKGTSVIRHTgespaacfptiqtpdcrlS 181
Cdd:cd21572   71 HPPSAATLHPPAAQPPEEQHLSA--------------------ETAASQQRFQCTSVIRHT------------------A 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 182 DsregeeqllghfetlqdthltdsllstnlvsCQPClhksggllltdkgqqagwpgavqTCSPKNyENDLPRKTTPLISV 261
Cdd:cd21572  113 D-------------------------------AQPC-----------------------SCSSCP-SSPSVVPSVPAGVA 137

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148161 262 SVPAPPVLCQMIPVTGQSSMLPAFLKPPPQLSvgtvrpilAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANV 341
Cdd:cd21572  138 GVSPVPVYCQILPVSSSSTTVVAAQAPLPQPQ--------QQAASPAQVFLMGGQVPKGPVMFLVPQPVVPTLYVQPTLV 209

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 295148161 342 MAAGnTKLLPLAPAPVFITSSQNCVP-QVDFSRRRN 376
Cdd:cd21572  210 TPGG-TKLAAIAPAPGHTPSEQRKSPpQPEVSRVRS 244

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 295148161  393 HLKAHLRTHTGEKPFNCswDGCDKKFAR 420
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 295148161  437 FVCPVCDRRFMRSDHLTKHARRH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295148161 403 GEKPFNCSWDGCDKKFARSDELSRHR-------RTH------------TGEKKFVCPVCDRRFMRSDHLTKHaRRHMT 461
Cdd:COG5189  346 DGKPYKCPVEGCNKKYKNQNGLKYHMlhghqnqKLHenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKHSH 422

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 295148161  407 FNCswDGCDKKFARSDELSRHRRTH 431
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23