NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|9968469|emb|CAC06697|]
View 

Kruppel like factor [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 15820645)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940
SCOP:  4003583

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KLF9_13_N-like super family cl41730
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 7-168 4.04e-21

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.


The actual alignment was detected with superfamily member cd21571:

Pssm-ID: 425361 [Multi-domain]  Cd Length: 136  Bit Score: 86.67  E-value: 4.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469    7 VDHFAASasCPCQPRSRA---RAAGRPEPRPEGAAAAAPtlPRVDERRDGKDSASLFVVARILADLNQQAPAPAPAERRE 83
Cdd:cd21571   1 VDHFAAE--CLVSMSSRAivhGPKGNPEPKPASEAAPPP--ENGEDRREGKDNSSLFVVARILADLNQQVPKPSAEQEKS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469   84 GAAARKARTPCRLppappapppgpepaspgqagapaaPPSPAWSEPeAALEQEPGPAGSGEPGLRQRGRRGRSRADLESP 163
Cdd:cd21571  77 NESAPREGEEPPL------------------------PAGKGGDGS-AATPTSPGGAAAAPPTPKQRSRRGRGRSDPESP 131


                ....*
gi 9968469  164 QRKHK 168
Cdd:cd21571 132 QKKHK 136
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-252 4.42e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 4.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469  162 SPQRKHKCHYAGCEKVYGKSSHLKAHLRTHTGERPFACSWQECNKKF-----ARSDELARHYRTHTGEKKFSC--PICEK 234
Cdd:COG5048 317 ESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSETlsNSCIR 396

                        90
                ....*....|....*...
gi 9968469  235 RFMRSDHLTKHARRHANF 252
Cdd:COG5048 397 NFKRDSNLSLHIITHLSF 414
 
Name Accession Description Interval E-value
KLF13_N cd21571
N-terminal domain of Kruppel-like factor 13; Kruppel-like factor 13 (KLF13; also known as ...
 7-168 4.04e-21

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: 86.67  E-value: 4.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469    7 VDHFAASasCPCQPRSRA---RAAGRPEPRPEGAAAAAPtlPRVDERRDGKDSASLFVVARILADLNQQAPAPAPAERRE 83
Cdd:cd21571   1 VDHFAAE--CLVSMSSRAivhGPKGNPEPKPASEAAPPP--ENGEDRREGKDNSSLFVVARILADLNQQVPKPSAEQEKS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469   84 GAAARKARTPCRLppappapppgpepaspgqagapaaPPSPAWSEPeAALEQEPGPAGSGEPGLRQRGRRGRSRADLESP 163
Cdd:cd21571  77 NESAPREGEEPPL------------------------PAGKGGDGS-AATPTSPGGAAAAPPTPKQRSRRGRGRSDPESP 131


                ....*
gi 9968469  164 QRKHK 168
Cdd:cd21571 132 QKKHK 136
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-252 4.42e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 4.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469  162 SPQRKHKCHYAGCEKVYGKSSHLKAHLRTHTGERPFACSWQECNKKF-----ARSDELARHYRTHTGEKKFSC--PICEK 234
Cdd:COG5048 317 ESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSETlsNSCIR 396

                        90
                ....*....|....*...
gi 9968469  235 RFMRSDHLTKHARRHANF 252
Cdd:COG5048 397 NFKRDSNLSLHIITHLSF 414
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 227-249 2.01e-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: 37.66  E-value: 2.01e-04
                          10        20
                  ....*....|....*....|...
gi 9968469    227 FSCPICEKRFMRSDHLTKHARRH 249
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF13_N cd21571
N-terminal domain of Kruppel-like factor 13; Kruppel-like factor 13 (KLF13; also known as ...
 7-168 4.04e-21

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: 86.67  E-value: 4.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469    7 VDHFAASasCPCQPRSRA---RAAGRPEPRPEGAAAAAPtlPRVDERRDGKDSASLFVVARILADLNQQAPAPAPAERRE 83
Cdd:cd21571   1 VDHFAAE--CLVSMSSRAivhGPKGNPEPKPASEAAPPP--ENGEDRREGKDNSSLFVVARILADLNQQVPKPSAEQEKS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469   84 GAAARKARTPCRLppappapppgpepaspgqagapaaPPSPAWSEPeAALEQEPGPAGSGEPGLRQRGRRGRSRADLESP 163
Cdd:cd21571  77 NESAPREGEEPPL------------------------PAGKGGDGS-AATPTSPGGAAAAPPTPKQRSRRGRGRSDPESP 131


                ....*
gi 9968469  164 QRKHK 168
Cdd:cd21571 132 QKKHK 136
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 23-168 1.59e-09

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: 55.85  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469   23 RARAAGRPEPRPEGAAAAAPTLPRVDERRDGKDSASLFVVARILADLNQQAPAPAPAERREGAAARKARTPCRLPPAPPA 102
Cdd:cd21975  27 GAGLAAGLDVRATREVAKGPGPPGPAWKPDGADSPGLVTAAPHLLAANVLAPLRGPSVEGSSLESGDADMGSDSDVAPAS 106

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9968469  103 PPPGPEPASPGQAGApaappspawSEPEAALEQEPGPAGSGEPGLRQRGRRGRSRADLESPQRKHK 168
Cdd:cd21975 107 GAAASTSPESSSDAA---------SSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAAKRHK 163
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-252 4.42e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 4.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469  162 SPQRKHKCHYAGCEKVYGKSSHLKAHLRTHTGERPFACSWQECNKKF-----ARSDELARHYRTHTGEKKFSC--PICEK 234
Cdd:COG5048 317 ESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSETlsNSCIR 396

                        90
                ....*....|....*...
gi 9968469  235 RFMRSDHLTKHARRHANF 252
Cdd:COG5048 397 NFKRDSNLSLHIITHLSF 414
KLF9_N cd21578
N-terminal domain of Kruppel-like factor 9; Kruppel-like factor 9 (KLF9; also known as ...
 3-79 2.08e-05

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.


Pssm-ID: 409239  Cd Length: 142  Bit Score: 43.64  E-value: 2.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9968469    3 AAAYVDHFAASASCPCQPRSRARAAGRPEPRPEGAAAAAPTLPRVDERRD-GKDSASLFVVARILADLNQQAPAPAPA 79
Cdd:cd21578   1 AVAYMDFVAAQCLVSISNRAAVPEHGRAPEPPEQRLPEREVTKEHGDPGDaWKDYCTLLTIAKSLLDLNKYRPLPSPS 78
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
181-232 8.05e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 8.05e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9968469  181 SSHLKAHLRTHTGERPFACSWQECNKKFARSDELARHYRTHTGEKKFSCPIC 232
Cdd:COG5048  46 LEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKS 97
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-287 1.20e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469  199 CSWQECNKKFARSDELARHYRT--HTGE--KKFSCPI--CEKRFMRSDHLTKHARRH--ANFHPGMLQRRG-------GG 263
Cdd:COG5048 290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHtsISPAKEKLLNSSskfspllNN 369

                        90       100
                ....*....|....*....|....
gi 9968469  264 SRTGSLSDYSRSDASSPTISPASS 287
Cdd:COG5048 370 EPPQSLQQYKDLKNDKKSETLSNS 393
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 227-249 2.01e-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: 37.66  E-value: 2.01e-04
                          10        20
                  ....*....|....*....|...
gi 9968469    227 FSCPICEKRFMRSDHLTKHARRH 249
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
195-288 4.54e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469  195 RPFACSwqECNKKFARSDELARHYRTHTGEKKFSC--PICEKRFMRSDHLTKHARRHANFHPgMLQRRGGGSRTGSLSDY 272
Cdd:COG5048  32 RPDSCP--NCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS-DLNSKSLPLSNSKASSS 108

                        90
                ....*....|....*.
gi 9968469  273 SRSDASSPTISPASSP 288
Cdd:COG5048 109 SLSSSSSNSNDNNLLS 124
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-245 5.93e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 5.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968469  162 SPQRKHKCHYAGCEKVYGKSSHLKAHLRTHTGERPFACSWQECNKKFARSDELARHYRTHTgEKKFSCPICEKRFMRSDH 241
Cdd:COG5048 382 KNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLD 460


                ....
gi 9968469  242 LTKH 245
Cdd:COG5048 461 LSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
183-210 1.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|....*...
gi 9968469    183 HLKAHLRTHTGERPFACswQECNKKFAR 210
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 167-191 7.56e-03

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: 33.43  E-value: 7.56e-03
                          10        20
                  ....*....|....*....|....*
gi 9968469    167 HKCHYagCEKVYGKSSHLKAHLRTH 191
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH