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Conserved domains on  [gi|12644412|sp|Q13887|]
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RecName: Full=Krueppel-like factor 5; AltName: Full=Basic transcription element-binding protein 2; Short=BTE-binding protein 2; AltName: Full=Colon krueppel-like factor; AltName: Full=GC-box-binding protein 2; AltName: Full=Intestinal-enriched krueppel-like factor; AltName: Full=Transcription factor BTEB2

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 3-370 2.66e-101

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. 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 KLF5.


:

Pssm-ID: 410335  Cd Length: 273  Bit Score: 303.75  E-value: 2.66e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412   3 TRVLSMSArlgpvpqPPAPQDEPVFAQLKPVLGAANPARDAALFPGEelkhahhrpqaqpapaqapqpaqpPATGPRLPP 82
Cdd:cd21579   1 AAGLRMSA-------GLAPGEEAVFTQLKPVLMSGGDGEESLLFGDK------------------------PAVRGRSSP 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412  83 EDLVQTRCEMEKYLTPQLPPVPIiPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTHIK 162
Cdd:cd21579  50 HDYNQTKSEMDKYLSPQPPPPPA-PEDKKYRRESASVVDEFFSEDKGSPYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPK 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 163 TEPVAIFSHQSettaPPPAPTQALPEFTSIFSSHQTAapeVNNIFIKQELPTPDLHlsvptQQGHLYQLLNTPDLDmpss 242
Cdd:cd21579 129 HEPPPPTSFCS----SSNGTTQALPEFTSVFSAPQSA---VNNVFIKQEMPSFDDQ-----QQGPLFQLLNSDLDQ---- 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 243 tnqtaamdtlnvsmsaamaglnthtsavpqtavkqfqgmppctytmpsqflPQQATYFPPSPPSSEPGSPDRQAEMLQNL 322
Cdd:cd21579 193 ---------------------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNL 221

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 12644412 323 TPPPSYAATIASKLAIHNPNLP----TTLPVNSQNIQPVRYNRRSNPDLEKR 370
Cdd:cd21579 222 SPPPSYAASIASKLAGQTPGLPppgvGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 433-455 6.99e-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: 39.59  E-value: 6.99e-05
                          10        20
                  ....*....|....*....|...
gi 12644412   433 FQCGVCNRSFSRSDHLALHMKRH 455
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-433 2.97e-04

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 2.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12644412 359 YNRRSNPDLEKRRIHYCdyPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 433
Cdd:COG5048  20 PKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
 
Name Accession Description Interval E-value
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 3-370 2.66e-101

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. 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 KLF5.


Pssm-ID: 410335  Cd Length: 273  Bit Score: 303.75  E-value: 2.66e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412   3 TRVLSMSArlgpvpqPPAPQDEPVFAQLKPVLGAANPARDAALFPGEelkhahhrpqaqpapaqapqpaqpPATGPRLPP 82
Cdd:cd21579   1 AAGLRMSA-------GLAPGEEAVFTQLKPVLMSGGDGEESLLFGDK------------------------PAVRGRSSP 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412  83 EDLVQTRCEMEKYLTPQLPPVPIiPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTHIK 162
Cdd:cd21579  50 HDYNQTKSEMDKYLSPQPPPPPA-PEDKKYRRESASVVDEFFSEDKGSPYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPK 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 163 TEPVAIFSHQSettaPPPAPTQALPEFTSIFSSHQTAapeVNNIFIKQELPTPDLHlsvptQQGHLYQLLNTPDLDmpss 242
Cdd:cd21579 129 HEPPPPTSFCS----SSNGTTQALPEFTSVFSAPQSA---VNNVFIKQEMPSFDDQ-----QQGPLFQLLNSDLDQ---- 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 243 tnqtaamdtlnvsmsaamaglnthtsavpqtavkqfqgmppctytmpsqflPQQATYFPPSPPSSEPGSPDRQAEMLQNL 322
Cdd:cd21579 193 ---------------------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNL 221

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 12644412 323 TPPPSYAATIASKLAIHNPNLP----TTLPVNSQNIQPVRYNRRSNPDLEKR 370
Cdd:cd21579 222 SPPPSYAASIASKLAGQTPGLPppgvGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 433-455 6.99e-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: 39.59  E-value: 6.99e-05
                          10        20
                  ....*....|....*....|...
gi 12644412   433 FQCGVCNRSFSRSDHLALHMKRH 455
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-433 2.97e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 2.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12644412 359 YNRRSNPDLEKRRIHYCdyPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 433
Cdd:COG5048  20 PKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
419-444 3.59e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.59e-04
                          10        20
                  ....*....|....*....|....*.
gi 12644412   419 ELTRHYRKHTGAKPFQCGVCNRSFSR 444
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-451 6.33e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 6.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 155 RPCVTHIKTEPVAIFSHQSETTAPPPAPTQALPEFTSIFSSHqtaAPEVNNIFIKQELPTPDLHLSVPTQQGHLYQLLNT 234
Cdd:COG5048 173 ANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSS---SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 235 PDlDMPSSTNQTAAMDTLNVSMSaaMAGLNTHTSAVPQTAVKQFQgMPPC--TYTMPSQFLPQQATYF----PPSPPSSE 308
Cdd:COG5048 250 SS-DSSSSASESPRSSLPTASSQ--SSSPNESDSSSEKGFSLPIK-SKQCniSFSRSSPLTRHLRSVNhsgeSLKPFSCP 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 309 PGSPDRQAEMLQNLTPPPSyaaTIASKLAIHNPNLPTTLPVNSQNIQPVRYNRRSNPDLEKRRIHYCDYPGCTKVYTKSS 388
Cdd:COG5048 326 YSLCGKLFSRNDALKRHIL---LHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDS 402

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12644412 389 HLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPFQCgVCNRSFSRSDHLALH 451
Cdd:COG5048 403 NLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLSNH 464
 
Name Accession Description Interval E-value
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 3-370 2.66e-101

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. 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 KLF5.


Pssm-ID: 410335  Cd Length: 273  Bit Score: 303.75  E-value: 2.66e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412   3 TRVLSMSArlgpvpqPPAPQDEPVFAQLKPVLGAANPARDAALFPGEelkhahhrpqaqpapaqapqpaqpPATGPRLPP 82
Cdd:cd21579   1 AAGLRMSA-------GLAPGEEAVFTQLKPVLMSGGDGEESLLFGDK------------------------PAVRGRSSP 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412  83 EDLVQTRCEMEKYLTPQLPPVPIiPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTHIK 162
Cdd:cd21579  50 HDYNQTKSEMDKYLSPQPPPPPA-PEDKKYRRESASVVDEFFSEDKGSPYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPK 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 163 TEPVAIFSHQSettaPPPAPTQALPEFTSIFSSHQTAapeVNNIFIKQELPTPDLHlsvptQQGHLYQLLNTPDLDmpss 242
Cdd:cd21579 129 HEPPPPTSFCS----SSNGTTQALPEFTSVFSAPQSA---VNNVFIKQEMPSFDDQ-----QQGPLFQLLNSDLDQ---- 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 243 tnqtaamdtlnvsmsaamaglnthtsavpqtavkqfqgmppctytmpsqflPQQATYFPPSPPSSEPGSPDRQAEMLQNL 322
Cdd:cd21579 193 ---------------------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNL 221

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 12644412 323 TPPPSYAATIASKLAIHNPNLP----TTLPVNSQNIQPVRYNRRSNPDLEKR 370
Cdd:cd21579 222 SPPPSYAASIASKLAGQTPGLPppgvGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 433-455 6.99e-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: 39.59  E-value: 6.99e-05
                          10        20
                  ....*....|....*....|...
gi 12644412   433 FQCGVCNRSFSRSDHLALHMKRH 455
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-433 2.97e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 2.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12644412 359 YNRRSNPDLEKRRIHYCdyPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 433
Cdd:COG5048  20 PKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
419-444 3.59e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.59e-04
                          10        20
                  ....*....|....*....|....*.
gi 12644412   419 ELTRHYRKHTGAKPFQCGVCNRSFSR 444
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-451 6.33e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 6.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 155 RPCVTHIKTEPVAIFSHQSETTAPPPAPTQALPEFTSIFSSHqtaAPEVNNIFIKQELPTPDLHLSVPTQQGHLYQLLNT 234
Cdd:COG5048 173 ANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSS---SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 235 PDlDMPSSTNQTAAMDTLNVSMSaaMAGLNTHTSAVPQTAVKQFQgMPPC--TYTMPSQFLPQQATYF----PPSPPSSE 308
Cdd:COG5048 250 SS-DSSSSASESPRSSLPTASSQ--SSSPNESDSSSEKGFSLPIK-SKQCniSFSRSSPLTRHLRSVNhsgeSLKPFSCP 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 309 PGSPDRQAEMLQNLTPPPSyaaTIASKLAIHNPNLPTTLPVNSQNIQPVRYNRRSNPDLEKRRIHYCDYPGCTKVYTKSS 388
Cdd:COG5048 326 YSLCGKLFSRNDALKRHIL---LHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDS 402

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12644412 389 HLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPFQCgVCNRSFSRSDHLALH 451
Cdd:COG5048 403 NLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-416 1.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|....*...
gi 12644412   389 HLKAHLRTHTGEKPYKCtwEGCDWRFAR 416
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 ...
 403-427 4.01e-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: 34.58  E-value: 4.01e-03
                          10        20
                  ....*....|....*....|....*
gi 12644412   403 YKCTweGCDWRFARSDELTRHYRKH 427
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 433-455 8.52e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 33.77  E-value: 8.52e-03
                          10        20
                  ....*....|....*....|...
gi 12644412   433 FQCGVCNRSFSRSDHLALHMKRH 455
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 360-453 8.86e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.16  E-value: 8.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12644412 360 NRRSNPDLEKRRIHYCDYPGcTKVYTKsshlkahlrthtGEKPYKCTWEGCDWRFARSDELTRHyRKH------------ 427
Cdd:COG5189 320 NSSSNGKLAHGGERNIDTPS-RMLKVK------------DGKPYKCPVEGCNKKYKNQNGLKYH-MLHghqnqklhenps 385

                        90       100       110
                ....*....|....*....|....*....|....
gi 12644412 428 --------TGAKPFQCGVCNRSFSRSDHLALHMK 453
Cdd:COG5189 386 pekmnifsAKDKPYRCEVCDKRYKNLNGLKYHRK 419
 
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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