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Conserved domains on  [gi|401709922|ref|NP_001257873|]
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Krueppel-like factor 7 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF6_7_N-like super family cl41732
N-terminal domain of Kruppel-like factor (KLF) 6, KLF7, and similar proteins; This subfamily ...
 7-192 8.41e-65

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.


The actual alignment was detected with superfamily member cd21585:

Pssm-ID: 425363  Cd Length: 160  Bit Score: 199.65  E-value: 8.41e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922   7 TCLELERYLQTEPRRISETFGEDLDCFLHASPPPCIEESFRRLDPLLLPVEAAICekssavDILLSRDKLLSETCLSLQP 86
Cdd:cd21585   34 TCLELERYLQTEPKRLSELFDEELDCLLTPSFLKEDEEEELRDPLLPLPVDEPPV------DILVSLDKLLSLLPSTLQT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922  87 ASSSLDSYTAVNQAQLNAVTSLTPPSSPELSRHLVKTSqtlsavdgtvtlklvakkaalssvkvggvataaaavtaagav 166
Cdd:cd21585  108 TSSSAEAYTGVNAAQLNAVTSLTPPSSPELGRHLVKPP------------------------------------------ 145

                        170       180
                 ....*....|....*....|....*.
gi 401709922 167 ksgqsdsdqggLGAEACPENKKRVHR 192
Cdd:cd21585  146 -----------GGGEDSPENKKRVHR 160
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 251-273 6.88e-05

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.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.21  E-value: 6.88e-05
                          10        20
                  ....*....|....*....|...
gi 401709922  251 FKCNHCDRCFSRSDHLALHMKRH 273
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-256 1.26e-04

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401709922 184 PENKKRVHRCQFNGCRKvyTKSSHLKAHQRTHTGEKPYKCSWEGCEWRFARSDELTRHYRKHTGAKPFKCNHC 256
Cdd:COG5048   27 LSNAPRPDSCPNCTDSF--SRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKS 97
 
Name Accession Description Interval E-value
KLF7_N cd21585
N-terminal domain of Kruppel-like factor 7; Kruppel-like factor 7 (KLF7; also known as ...
 7-192 8.41e-65

N-terminal domain of Kruppel-like factor 7; Kruppel-like factor 7 (KLF7; also known as Krueppel-like factor 7, or ubiquitous Kruppel-like factor/UKLF) is a protein which, in humans, is encoded by the KLF7 gene. 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. It 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 KLF7.


Pssm-ID: 409244  Cd Length: 160  Bit Score: 199.65  E-value: 8.41e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922   7 TCLELERYLQTEPRRISETFGEDLDCFLHASPPPCIEESFRRLDPLLLPVEAAICekssavDILLSRDKLLSETCLSLQP 86
Cdd:cd21585   34 TCLELERYLQTEPKRLSELFDEELDCLLTPSFLKEDEEEELRDPLLPLPVDEPPV------DILVSLDKLLSLLPSTLQT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922  87 ASSSLDSYTAVNQAQLNAVTSLTPPSSPELSRHLVKTSqtlsavdgtvtlklvakkaalssvkvggvataaaavtaagav 166
Cdd:cd21585  108 TSSSAEAYTGVNAAQLNAVTSLTPPSSPELGRHLVKPP------------------------------------------ 145

                        170       180
                 ....*....|....*....|....*.
gi 401709922 167 ksgqsdsdqggLGAEACPENKKRVHR 192
Cdd:cd21585  146 -----------GGGEDSPENKKRVHR 160
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 251-273 6.88e-05

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.21  E-value: 6.88e-05
                          10        20
                  ....*....|....*....|...
gi 401709922  251 FKCNHCDRCFSRSDHLALHMKRH 273
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-256 1.26e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401709922 184 PENKKRVHRCQFNGCRKvyTKSSHLKAHQRTHTGEKPYKCSWEGCEWRFARSDELTRHYRKHTGAKPFKCNHC 256
Cdd:COG5048   27 LSNAPRPDSCPNCTDSF--SRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKS 97
zf-H2C2_2 pfam13465
Zinc-finger double domain;
237-262 2.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 2.04e-04
                          10        20
                  ....*....|....*....|....*.
gi 401709922  237 ELTRHYRKHTGAKPFKCNHCDRCFSR 262
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KLF7_N cd21585
N-terminal domain of Kruppel-like factor 7; Kruppel-like factor 7 (KLF7; also known as ...
 7-192 8.41e-65

N-terminal domain of Kruppel-like factor 7; Kruppel-like factor 7 (KLF7; also known as Krueppel-like factor 7, or ubiquitous Kruppel-like factor/UKLF) is a protein which, in humans, is encoded by the KLF7 gene. 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. It 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 KLF7.


Pssm-ID: 409244  Cd Length: 160  Bit Score: 199.65  E-value: 8.41e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922   7 TCLELERYLQTEPRRISETFGEDLDCFLHASPPPCIEESFRRLDPLLLPVEAAICekssavDILLSRDKLLSETCLSLQP 86
Cdd:cd21585   34 TCLELERYLQTEPKRLSELFDEELDCLLTPSFLKEDEEEELRDPLLPLPVDEPPV------DILVSLDKLLSLLPSTLQT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922  87 ASSSLDSYTAVNQAQLNAVTSLTPPSSPELSRHLVKTSqtlsavdgtvtlklvakkaalssvkvggvataaaavtaagav 166
Cdd:cd21585  108 TSSSAEAYTGVNAAQLNAVTSLTPPSSPELGRHLVKPP------------------------------------------ 145

                        170       180
                 ....*....|....*....|....*.
gi 401709922 167 ksgqsdsdqggLGAEACPENKKRVHR 192
Cdd:cd21585  146 -----------GGGEDSPENKKRVHR 160
KLF6_7_N-like cd21973
N-terminal domain of Kruppel-like factor (KLF) 6, KLF7, and similar proteins; This subfamily ...
 7-129 7.90e-15

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.


Pssm-ID: 409246 [Multi-domain]  Cd Length: 138  Bit Score: 69.61  E-value: 7.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922   7 TCLELERYLQTEPRRISETFGE-DLDCFLHASPPPCIEESFRRLDplllpveaaicekssavDILLSRDKLLSETCLSLQ 85
Cdd:cd21973   34 TCYEMERYLKDEPKLTSYKKDPsDSPWSPWDLFTPPSEESESSDS-----------------DLSLLSIDDLLLDVSSLS 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 401709922  86 PASSSLDSytavnqaqlnavTSLTPPSSPELSRHLVKTSQTLSA 129
Cdd:cd21973   97 SSSSSSSG------------VSWTPPSSPESSRSHPSSSYTKSS 128
KLF6_N cd21586
N-terminal domain of Kruppel-like factor 6; Kruppel-like factor 6 (KLF6; also known as ...
 7-192 1.71e-06

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.


Pssm-ID: 409245  Cd Length: 198  Bit Score: 47.38  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922   7 TCLELERYLQTEPRRISETFG-----EDL------DCFLHASPPPCIEESFRRLDPLLLPVEAAICEKSSAVDILLSRDK 75
Cdd:cd21586   34 TCLELERYLQSEPYVSAADLRkfdgqEDLwsklilACGDKGESSPKIPSSSEEDIQDSQNLETNSFNSDASSEASDSSEE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709922  76 LLSETCLSLQPASSSLdsytaVNQAQLNAVTSLTPPSSPELSrhlvktsqtlsavdgtvtlKLVAKKAALSSVkvggvat 155
Cdd:cd21586  114 LSPTLSFTSNPLSDVL-----VNSGHLGSSVISTPPSSPELA-------------------KEPSAPLAWGVG------- 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 401709922 156 aAAAVTAAGAVKSGQSDSDQGGLGAEACPENKKRVHR 192
Cdd:cd21586  163 -GAALSSGGGGRGGKSAERGGEGGGEASPDGRRRVHR 198
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 251-273 6.88e-05

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.21  E-value: 6.88e-05
                          10        20
                  ....*....|....*....|...
gi 401709922  251 FKCNHCDRCFSRSDHLALHMKRH 273
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-256 1.26e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401709922 184 PENKKRVHRCQFNGCRKvyTKSSHLKAHQRTHTGEKPYKCSWEGCEWRFARSDELTRHYRKHTGAKPFKCNHC 256
Cdd:COG5048   27 LSNAPRPDSCPNCTDSF--SRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKS 97
zf-H2C2_2 pfam13465
Zinc-finger double domain;
237-262 2.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 2.04e-04
                          10        20
                  ....*....|....*....|....*.
gi 401709922  237 ELTRHYRKHTGAKPFKCNHCDRCFSR 262
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
196-253 9.66e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 9.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401709922 196 NGCRKVYTKSSHLKAHQRT--HTGE--KPYKCSWEGCEWRFARSDELTRHYRKHTGAKPFKC 253
Cdd:COG5048  293 KQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE 354
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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