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Conserved domains on  [gi|144922690|ref|NP_510962|]
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Krueppel-like factor 16 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF16_N cd21573
N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as ...
 2-127 1.80e-29

N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as Krueppel-like factor 16, Basic transcription element binding protein 4/BTEB4, or Novel Sp1-like zinc finger transcription factor/2NSLP2) is a protein that in humans is encoded by the KLF16 gene. KLF16 functions as a transcription activator. It is thought to modulate dopaminergic transmission in the brain and also regulates the expression of several genes essential for metabolic and endocrine processes in sex steroid-sensitive uterine cells. KLF16 selectively binds three distinct KLF-binding sites (GC, CA, and BTE boxes). 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. KLF16 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 KLF16.


:

Pssm-ID: 409237 [Multi-domain]  Cd Length: 125  Bit Score: 107.38  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATP-PGTPGAPPPPATAPGPGGATAAPHLLAA 80
Cdd:cd21573    1 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAPRREAAPpGTPGPPPPPPAPSPPPGGAAAAPHLLAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 144922690  81 SILADLRGGPVVAtaastAGGTSPVSSSSAASSPSSGRAPG---AAKSHR 127
Cdd:cd21573   81 SILADLRGGPGAA-----PGGASPASSSSAASSPSSGRAPGaaaAAKSHR 125
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
124-186 7.13e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 7.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 144922690 124 KSHRCPFhgCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTGEKRF 186
Cdd:COG5048   32 RPDSCPN--CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 186-208 3.51e-04

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: 36.89  E-value: 3.51e-04
                          10        20
                  ....*....|....*....|...
gi 144922690  186 FPCPLCTKRFTRSDHLTKHARRH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF16_N cd21573
N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as ...
 2-127 1.80e-29

N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as Krueppel-like factor 16, Basic transcription element binding protein 4/BTEB4, or Novel Sp1-like zinc finger transcription factor/2NSLP2) is a protein that in humans is encoded by the KLF16 gene. KLF16 functions as a transcription activator. It is thought to modulate dopaminergic transmission in the brain and also regulates the expression of several genes essential for metabolic and endocrine processes in sex steroid-sensitive uterine cells. KLF16 selectively binds three distinct KLF-binding sites (GC, CA, and BTE boxes). 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. KLF16 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 KLF16.


Pssm-ID: 409237 [Multi-domain]  Cd Length: 125  Bit Score: 107.38  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATP-PGTPGAPPPPATAPGPGGATAAPHLLAA 80
Cdd:cd21573    1 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAPRREAAPpGTPGPPPPPPAPSPPPGGAAAAPHLLAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 144922690  81 SILADLRGGPVVAtaastAGGTSPVSSSSAASSPSSGRAPG---AAKSHR 127
Cdd:cd21573   81 SILADLRGGPGAA-----PGGASPASSSSAASSPSSGRAPGaaaAAKSHR 125
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
124-186 7.13e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 7.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 144922690 124 KSHRCPFhgCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTGEKRF 186
Cdd:COG5048   32 RPDSCPN--CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
172-197 1.29e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 1.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 144922690  172 ELARHHRTHTGEKRFPCPLCTKRFTR 197
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 186-208 3.51e-04

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: 36.89  E-value: 3.51e-04
                          10        20
                  ....*....|....*....|...
gi 144922690  186 FPCPLCTKRFTRSDHLTKHARRH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
158-231 6.75e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690 158 CDWPGCDKKFARSDELARHHRT--HTGE--KRFPCP--LCTKRFTRSDHLTKHARRHPG--FRPELLRRPGARSVSPSDS 229
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSisPAKEKLLNSSSKFSPLLNN 369


                 ..
gi 144922690 230 LP 231
Cdd:COG5048  370 EP 371
 
Name Accession Description Interval E-value
KLF16_N cd21573
N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as ...
 2-127 1.80e-29

N-terminal domain of Kruppel-like factor 16; Kruppel-like factor 16 (KLF16; also known as Krueppel-like factor 16, Basic transcription element binding protein 4/BTEB4, or Novel Sp1-like zinc finger transcription factor/2NSLP2) is a protein that in humans is encoded by the KLF16 gene. KLF16 functions as a transcription activator. It is thought to modulate dopaminergic transmission in the brain and also regulates the expression of several genes essential for metabolic and endocrine processes in sex steroid-sensitive uterine cells. KLF16 selectively binds three distinct KLF-binding sites (GC, CA, and BTE boxes). 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. KLF16 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 KLF16.


Pssm-ID: 409237 [Multi-domain]  Cd Length: 125  Bit Score: 107.38  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATP-PGTPGAPPPPATAPGPGGATAAPHLLAA 80
Cdd:cd21573    1 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAPRREAAPpGTPGPPPPPPAPSPPPGGAAAAPHLLAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 144922690  81 SILADLRGGPVVAtaastAGGTSPVSSSSAASSPSSGRAPG---AAKSHR 127
Cdd:cd21573   81 SILADLRGGPGAA-----PGGASPASSSSAASSPSSGRAPGaaaAAKSHR 125
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 8-96 3.56e-17

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) 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. 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. 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 KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 76.27  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   8 VDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATPPGTPGAPPPPATAPGPGGATAAPHLLAASILADLR 87
Cdd:cd21975    1 VDYFAAECLVSISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGPGPPGPAWKPDGADSPGLVTAAPHLLAANVLAPLR 80


                 ....*....
gi 144922690  88 GGPVVATAA 96
Cdd:cd21975   81 GPSVEGSSL 89
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 2-89 3.72e-16

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.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 74.09  E-value: 3.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690   2 SAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREAT------PPGTPGAPPPPATAPGPGGATAAP 75
Cdd:cd21576    1 SAAVACLDYFAAECLVSMSAGAVLHRRAPDPEGAGGAAGSEVGAAPPESAlpgpgpPGPAWVPPLLQVPAPSPGAGGAAP 80

                         90
                 ....*....|....
gi 144922690  76 HLLAASILADLRGG 89
Cdd:cd21576   81 HLLAASVLADLRGG 94
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
124-186 7.13e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 7.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 144922690 124 KSHRCPFhgCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTGEKRF 186
Cdd:COG5048   32 RPDSCPN--CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
124-209 1.30e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690 124 KSHRCPfhGCAKAYYKSSHLKSHLRT--HTGE--RPFACDWPGCDKKFARSDELARHHRTHTGEKRFPCPL--CTKRFTR 197
Cdd:COG5048  288 LPIKSK--QCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSP 365

                         90
                 ....*....|..
gi 144922690 198 SDHLTKHARRHP 209
Cdd:COG5048  366 LLNNEPPQSLQQ 377
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
124-204 7.53e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690 124 KSHRCPFHGCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTgEKRFPCPLCTKRFTRSDHLTK 203
Cdd:COG5048  385 KKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSN 463


                 .
gi 144922690 204 H 204
Cdd:COG5048  464 H 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
172-197 1.29e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 1.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 144922690  172 ELARHHRTHTGEKRFPCPLCTKRFTR 197
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 152-208 4.61e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 4.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 144922690 152 GERPFACDWPGCDKKFARSDELaRHHRTH--------------------TGEKRFPCPLCTKRFTRSDHLTKHaRRH 208
Cdd:COG5189  346 DGKPYKCPVEGCNKKYKNQNGL-KYHMLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYH-RKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
142-169 1.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|....*...
gi 144922690  142 HLKSHLRTHTGERPFACdwPGCDKKFAR 169
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
KLF13_N cd21571
N-terminal domain of Kruppel-like factor 13; Kruppel-like factor 13 (KLF13; also known as ...
 8-49 2.78e-04

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.


Pssm-ID: 409236 [Multi-domain]  Cd Length: 136  Bit Score: 40.06  E-value: 2.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 144922690   8 VDYFAADVLMAISSGAVVHR------GRPGPEGAGPAAGLDVRATRRE 49
Cdd:cd21571    1 VDHFAAECLVSMSSRAIVHGpkgnpePKPASEAAPPPENGEDRREGKD 48
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 186-208 3.51e-04

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: 36.89  E-value: 3.51e-04
                          10        20
                  ....*....|....*....|...
gi 144922690  186 FPCPLCTKRFTRSDHLTKHARRH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
158-231 6.75e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144922690 158 CDWPGCDKKFARSDELARHHRT--HTGE--KRFPCP--LCTKRFTRSDHLTKHARRHPG--FRPELLRRPGARSVSPSDS 229
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSisPAKEKLLNSSSKFSPLLNN 369


                 ..
gi 144922690 230 LP 231
Cdd:COG5048  370 EP 371
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
154-209 1.13e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 1.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 144922690 154 RPFACdwPGCDKKFARSDELARHHRTHTGEKRFPC--PLCTKRFTRSDHLTKHARRHP 209
Cdd:COG5048   32 RPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHH 87
 
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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