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Conserved domains on  [gi|1580237686|ref|NP_034765|]
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Krueppel-like factor 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF1_N cd21581
N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as ...
 10-275 1.38e-74

N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as Krueppel-like factor 1 or Erythroid Kruppel-like Factor/EKLF) was the first Kruppel-like factor discovered. It was found to be vitally important for embryonic erythropoiesis in promoting the switch from fetal hemoglobin (Hemoglobin F) to adult hemoglobin (Hemoglobin A) gene expression by binding to highly conserved CACCC domains. EKLF ablation in mouse embryos produces a lethal anemic phenotype, causing death by embryonic day 14, and natural mutations lead to beta+ thalassemia in humans. However, expression of embryonic hemoglobin and fetal hemoglobin genes is normal in EKLF-deficient mice, suggesting other factors may be involved. KLF1 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 specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF1, which is related to the N-terminal domains of KLF2 and KLF4.


:

Pssm-ID: 409227 [Multi-domain]  Cd Length: 278  Bit Score: 231.86  E-value: 1.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  10 SISTLTTLGQFLDTQEDFLKWWRSEETQDLGPGPPNPTGPSHHVSLKSEDP-SGEDDERDVTCAWDPDLFLTNFPGS--E 86
Cdd:cd21581     1 AVLPSFSSFSFLDHQSDNMKVWKSEEGQLPLDGPPDKLSPSGSEQLQVSQPmTEELLDDDSQASWDIEFLLSNWSSPslN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  87 SPGTSRTCALAPSVGPVAQFEP-----PESLGAYAGGPGLVTGPLGSEEHTSWAHPTPRPPAPEPFVAPALAPGLAPKAQ 161
Cdd:cd21581    81 PSLDNNTQALPQEEQPGAYYEPpkkdqPGTEGLQVGGPGLMAELLSPEESTGWAPPEPHHGYPDAFVGPALFPAPANVDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 162 PSY------------SDSRAGSVGGFFPRAGLAVPAAPGAPYGLLSGYPALYPAPQYQGHFQLFRGLAAPSAGPTAPPsf 229
Cdd:cd21581   161 FGFpqggsvdrrgnlSKSGSWDFGSYYPQQHPSVVAFPDSRFGPLSGPQALTPDPQHYGYFQLFRHNAALFPDYAHSP-- 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1580237686 230 lnclGPGTVATELGATaiAGDAGLSPGTAPPKRSRRTLAPKRQAAH 275
Cdd:cd21581   239 ----GPGHLPLGQQPL--LPDPPLPPGGAEGKRGRRSWAKKRPAVH 278
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-357 7.28e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 279 HEGCGKSYTKSSHLKAHLRT--HTGE--KPYACSWDGCDWRFARSDELTRHYRKHTGHRPFCCGLCPRafSRSDHLALHM 354
Cdd:COG5048   292 SKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNS--SSKFSPLLNN 369


                  ...
gi 1580237686 355 KRH 357
Cdd:COG5048   370 EPP 372
 
Name Accession Description Interval E-value
KLF1_N cd21581
N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as ...
 10-275 1.38e-74

N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as Krueppel-like factor 1 or Erythroid Kruppel-like Factor/EKLF) was the first Kruppel-like factor discovered. It was found to be vitally important for embryonic erythropoiesis in promoting the switch from fetal hemoglobin (Hemoglobin F) to adult hemoglobin (Hemoglobin A) gene expression by binding to highly conserved CACCC domains. EKLF ablation in mouse embryos produces a lethal anemic phenotype, causing death by embryonic day 14, and natural mutations lead to beta+ thalassemia in humans. However, expression of embryonic hemoglobin and fetal hemoglobin genes is normal in EKLF-deficient mice, suggesting other factors may be involved. KLF1 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 specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF1, which is related to the N-terminal domains of KLF2 and KLF4.


Pssm-ID: 409227 [Multi-domain]  Cd Length: 278  Bit Score: 231.86  E-value: 1.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  10 SISTLTTLGQFLDTQEDFLKWWRSEETQDLGPGPPNPTGPSHHVSLKSEDP-SGEDDERDVTCAWDPDLFLTNFPGS--E 86
Cdd:cd21581     1 AVLPSFSSFSFLDHQSDNMKVWKSEEGQLPLDGPPDKLSPSGSEQLQVSQPmTEELLDDDSQASWDIEFLLSNWSSPslN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  87 SPGTSRTCALAPSVGPVAQFEP-----PESLGAYAGGPGLVTGPLGSEEHTSWAHPTPRPPAPEPFVAPALAPGLAPKAQ 161
Cdd:cd21581    81 PSLDNNTQALPQEEQPGAYYEPpkkdqPGTEGLQVGGPGLMAELLSPEESTGWAPPEPHHGYPDAFVGPALFPAPANVDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 162 PSY------------SDSRAGSVGGFFPRAGLAVPAAPGAPYGLLSGYPALYPAPQYQGHFQLFRGLAAPSAGPTAPPsf 229
Cdd:cd21581   161 FGFpqggsvdrrgnlSKSGSWDFGSYYPQQHPSVVAFPDSRFGPLSGPQALTPDPQHYGYFQLFRHNAALFPDYAHSP-- 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1580237686 230 lnclGPGTVATELGATaiAGDAGLSPGTAPPKRSRRTLAPKRQAAH 275
Cdd:cd21581   239 ----GPGHLPLGQQPL--LPDPPLPPGGAEGKRGRRSWAKKRPAVH 278
EKLF_TAD2 pfam16833
Erythroid krueppel-like transcription factor, transactivation 2; This family is the second ...
 63-85 7.42e-08

Erythroid krueppel-like transcription factor, transactivation 2; This family is the second part of the minimal transactivation domain of erythroid-specific transcription factor EKFL in craniates. EKLF plays an important role in red blood cell development; it is post-translationally modified by ubiquitin on several lysine residues, and its turnover in the cell is regulated by ubiquitin-mediated degradation. In the first 90 residues at the N-terminus EKLF carries a minimal transactivation or TAD domain that is highly acidic. This minimal TAD of EKLF can be further subdivided into two independent domains EKLF_TAD1 (residues 1-40), pfam16832, and EKLF_TAD2 (residues 51-90) that are both capable of independently activating transcription. Both TAD1 and TAD2 are highly acidic and carry a PEST (sequence rich in proline, glutamic acid, serine, and threonine) region. Deletion of either PEST domain significantly slows down degradation of EKLF by ubiquitin. The minimal TAD has an overlapping activation/degradation function that is critical for the role of EKLF in red blood cell development.


Pssm-ID: 407080  Cd Length: 27  Bit Score: 47.85  E-value: 7.42e-08
                          10        20
                  ....*....|....*....|...
gi 1580237686  63 EDDERDVTCAWDPDLFLTNFPGS 85
Cdd:pfam16833   5 EDDERDAAAAWDLDLFLTNFPGP 27
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-357 7.28e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 279 HEGCGKSYTKSSHLKAHLRT--HTGE--KPYACSWDGCDWRFARSDELTRHYRKHTGHRPFCCGLCPRafSRSDHLALHM 354
Cdd:COG5048   292 SKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNS--SSKFSPLLNN 369


                  ...
gi 1580237686 355 KRH 357
Cdd:COG5048   370 EPP 372
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 275-299 3.32e-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: 37.28  E-value: 3.32e-04
                          10        20
                  ....*....|....*....|....*
gi 1580237686 275 HTCGHegCGKSYTKSSHLKAHLRTH 299
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF1_N cd21581
N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as ...
 10-275 1.38e-74

N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as Krueppel-like factor 1 or Erythroid Kruppel-like Factor/EKLF) was the first Kruppel-like factor discovered. It was found to be vitally important for embryonic erythropoiesis in promoting the switch from fetal hemoglobin (Hemoglobin F) to adult hemoglobin (Hemoglobin A) gene expression by binding to highly conserved CACCC domains. EKLF ablation in mouse embryos produces a lethal anemic phenotype, causing death by embryonic day 14, and natural mutations lead to beta+ thalassemia in humans. However, expression of embryonic hemoglobin and fetal hemoglobin genes is normal in EKLF-deficient mice, suggesting other factors may be involved. KLF1 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 specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF1, which is related to the N-terminal domains of KLF2 and KLF4.


Pssm-ID: 409227 [Multi-domain]  Cd Length: 278  Bit Score: 231.86  E-value: 1.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  10 SISTLTTLGQFLDTQEDFLKWWRSEETQDLGPGPPNPTGPSHHVSLKSEDP-SGEDDERDVTCAWDPDLFLTNFPGS--E 86
Cdd:cd21581     1 AVLPSFSSFSFLDHQSDNMKVWKSEEGQLPLDGPPDKLSPSGSEQLQVSQPmTEELLDDDSQASWDIEFLLSNWSSPslN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  87 SPGTSRTCALAPSVGPVAQFEP-----PESLGAYAGGPGLVTGPLGSEEHTSWAHPTPRPPAPEPFVAPALAPGLAPKAQ 161
Cdd:cd21581    81 PSLDNNTQALPQEEQPGAYYEPpkkdqPGTEGLQVGGPGLMAELLSPEESTGWAPPEPHHGYPDAFVGPALFPAPANVDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 162 PSY------------SDSRAGSVGGFFPRAGLAVPAAPGAPYGLLSGYPALYPAPQYQGHFQLFRGLAAPSAGPTAPPsf 229
Cdd:cd21581   161 FGFpqggsvdrrgnlSKSGSWDFGSYYPQQHPSVVAFPDSRFGPLSGPQALTPDPQHYGYFQLFRHNAALFPDYAHSP-- 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1580237686 230 lnclGPGTVATELGATaiAGDAGLSPGTAPPKRSRRTLAPKRQAAH 275
Cdd:cd21581   239 ----GPGHLPLGQQPL--LPDPPLPPGGAEGKRGRRSWAKKRPAVH 278
KLF1_2_4_N cd21972
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ...
 10-275 2.49e-20

N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, 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. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity 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 KLF1, KLF2, KLF4, and similar proteins.


Pssm-ID: 409230 [Multi-domain]  Cd Length: 194  Bit Score: 87.35  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  10 SISTLTTLGQFLDTQEDFLKWWRSEETQdlgpgppnptgpshhvslksedPSGEDDERDVTCAWDPDLFLTNFPGSESPG 89
Cdd:cd21972     1 SESSLVSSGPFAKPEDDLSKFLDLEFIL----------------------SNTVTSDNDNPPPPDPAYPPPESPESCSTV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686  90 tsrtcalAPSVGPvaqfEPPESLGAYAGGPGLVTGPLGSeehtswahptprppapepFVAPALAPGLAPKAQPSYSDSRA 169
Cdd:cd21972    59 -------YDSDGC----HPTPNAYCGPNGPGLPGHFLLA------------------GNSPNLGPKIKTENQEQACMPVA 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 170 GSVGGFFPRAGLAVPAAPgapygllsgypalyPAPQYQGHFQLFRGLAAPSagptaPPSFLNCLGPGTVATELGATAIAG 249
Cdd:cd21972   110 GYSGHYGPREPQRVPPAP--------------PPPQYAGHFQYHGHFNMFS-----PPLRANHPGMSTVMLTPLSTPPLG 170

                         250       260
                  ....*....|....*....|....*.
gi 1580237686 250 daGLSPGTAPPKRSRRTLAPKRQAAH 275
Cdd:cd21972   171 --FLSPEEAKPKRGRRSWARKRTATH 194
EKLF_TAD2 pfam16833
Erythroid krueppel-like transcription factor, transactivation 2; This family is the second ...
 63-85 7.42e-08

Erythroid krueppel-like transcription factor, transactivation 2; This family is the second part of the minimal transactivation domain of erythroid-specific transcription factor EKFL in craniates. EKLF plays an important role in red blood cell development; it is post-translationally modified by ubiquitin on several lysine residues, and its turnover in the cell is regulated by ubiquitin-mediated degradation. In the first 90 residues at the N-terminus EKLF carries a minimal transactivation or TAD domain that is highly acidic. This minimal TAD of EKLF can be further subdivided into two independent domains EKLF_TAD1 (residues 1-40), pfam16832, and EKLF_TAD2 (residues 51-90) that are both capable of independently activating transcription. Both TAD1 and TAD2 are highly acidic and carry a PEST (sequence rich in proline, glutamic acid, serine, and threonine) region. Deletion of either PEST domain significantly slows down degradation of EKLF by ubiquitin. The minimal TAD has an overlapping activation/degradation function that is critical for the role of EKLF in red blood cell development.


Pssm-ID: 407080  Cd Length: 27  Bit Score: 47.85  E-value: 7.42e-08
                          10        20
                  ....*....|....*....|...
gi 1580237686  63 EDDERDVTCAWDPDLFLTNFPGS 85
Cdd:pfam16833   5 EDDERDAAAAWDLDLFLTNFPGP 27
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-357 7.28e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 279 HEGCGKSYTKSSHLKAHLRT--HTGE--KPYACSWDGCDWRFARSDELTRHYRKHTGHRPFCCGLCPRafSRSDHLALHM 354
Cdd:COG5048   292 SKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNS--SSKFSPLLNN 369


                  ...
gi 1580237686 355 KRH 357
Cdd:COG5048   370 EPP 372
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
280-350 7.74e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 7.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1580237686 280 EGCGKSYTKSSHLKAHLRTHTGEKPYACSWDGCDWRFARSDELTRHYRKHTGHRPFCC--GLCPRAFSRSDHL 350
Cdd:COG5048    37 PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSS 109
EKLF_TAD1 pfam16832
Erythroid krueppel-like transcription factor, transactivation 1; This family is the first part ...
 22-39 8.50e-07

Erythroid krueppel-like transcription factor, transactivation 1; This family is the first part of the minimal transactivation domain of erythroid-specific transcription factor EKFL in craniates. EKLF plays an important role in red blood cell development; it is posttranslationally modified by UBI on several lysine residues, and its turnover in the cell is regulated by ubiquitin-mediated degradation. In the first 90 residues at the N-terminus EKLF carries a minimal transactivation or TAD domain that is highly acidic. This minimal TAD of EKLF can be further subdivided into two independent domains EKLF_TAD1 (residues 1-40) and EKLF_TAD2 (residues 51-90), pfam16833, that are both capable of independently activating transcription. TAD1, is able to form a non-covalent interaction with ubiquitin. Both TAD1 and TAd2 are highly acidic and carry a PEST (sequence rich in proline, glutamic acid, serine, and threonine) region. Deletion of either PEST domain significantly slows down degradation of EKLF by ubiquitin. The minimal TAD has an overlapping activation/degradation function that is critical for the role of EKLF in red blood cell development.


Pssm-ID: 318931  Cd Length: 27  Bit Score: 44.70  E-value: 8.50e-07
                          10
                  ....*....|....*...
gi 1580237686  22 DTQEDFLKWWRSEETQDL 39
Cdd:pfam16832   1 DAQEDFLKWWHSEEEQDL 18
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
269-353 4.39e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580237686 269 PKRQAAHTCGHEGCGKSYTKSSHLKAHLRTHTGEKPYACSWDGCDWRFARSDELTRHYRKHTGHRPFCCGLCPRaFSRSD 348
Cdd:COG5048   381 LKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDL 459


                  ....*
gi 1580237686 349 HLALH 353
Cdd:COG5048   460 DLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 275-299 3.32e-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: 37.28  E-value: 3.32e-04
                          10        20
                  ....*....|....*....|....*
gi 1580237686 275 HTCGHegCGKSYTKSSHLKAHLRTH 299
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
291-318 1.17e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.17e-03
                          10        20
                  ....*....|....*....|....*...
gi 1580237686 291 HLKAHLRTHTGEKPYACswDGCDWRFAR 318
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 ...
 305-329 9.13e-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: 9.13e-03
                          10        20
                  ....*....|....*....|....*
gi 1580237686 305 YACswDGCDWRFARSDELTRHYRKH 329
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 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.
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