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Conserved domains on  [gi|1950476452|ref|XP_038271497|]
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Krueppel-like factor 5 isoform X2 [Dermochelys coriacea]

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 ...
 3-361 4.99e-123

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: 358.84  E-value: 4.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452   3 SSGLVLSTPN-LEESTVFTQLKPVRMSGESAEDTSVFEDiKPAIRILENQHDLAQltalrmeqrmpltmeARSEMDKYLS 81
Cdd:cd21579     1 AAGLRMSAGLaPGEEAVFTQLKPVLMSGGDGEESLLFGD-KPAVRGRSSPHDYNQ---------------TKSEMDKYLS 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452  82 SQLLPVPMVPDKKYRRESASVVDEFFSTEKPSstPYSVNINVILPDTTHLRTGLYRPAKPLTPFPQIKTEPGTSFtqpCS 161
Cdd:cd21579    65 PQPPPPPAPEDKKYRRESASVVDEFFSEDKGS--PYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPKHEPPPPTSF---CS 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 162 STAGSTQTLPDFTSVFSMPQSvAVNNIFIKQEMPSEIPlsgsLQQAQLYQMPIGNGDAdvatmvpstgsttaintisgvt 241
Cdd:cd21579   140 SSNGTTQALPEFTSVFSAPQS-AVNNVFIKQEMPSFDD----QQQGPLFQLLNSDLDQ---------------------- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 242 mstgsamlprhiqpggqvkhfqnvsqsqgnfnvtghfyPVPGLNLPPSPPNSQPGSPENQPELINTISPPPSYEATFGLK 321
Cdd:cd21579   193 --------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNLSPPPSYAASIASK 234

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1950476452 322 LVQSSQIPTLPNgLGTLSQGHIIMPTPKYNRRNNPELEKR 361
Cdd:cd21579   235 LAGQTPGLPPPG-VGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-H2C2_2 pfam13465
Zinc-finger double domain;
410-435 1.53e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 1950476452 410 ELTRHYRKHTGAKPFKCIACGRCFSR 435
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-407 4.21e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.21e-04
                          10        20
                  ....*....|....*....|....*...
gi 1950476452 380 HLKAHQRTHTGEKPYKCtwEGCDWRFAR 407
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
 
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 ...
 3-361 4.99e-123

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: 358.84  E-value: 4.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452   3 SSGLVLSTPN-LEESTVFTQLKPVRMSGESAEDTSVFEDiKPAIRILENQHDLAQltalrmeqrmpltmeARSEMDKYLS 81
Cdd:cd21579     1 AAGLRMSAGLaPGEEAVFTQLKPVLMSGGDGEESLLFGD-KPAVRGRSSPHDYNQ---------------TKSEMDKYLS 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452  82 SQLLPVPMVPDKKYRRESASVVDEFFSTEKPSstPYSVNINVILPDTTHLRTGLYRPAKPLTPFPQIKTEPGTSFtqpCS 161
Cdd:cd21579    65 PQPPPPPAPEDKKYRRESASVVDEFFSEDKGS--PYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPKHEPPPPTSF---CS 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 162 STAGSTQTLPDFTSVFSMPQSvAVNNIFIKQEMPSEIPlsgsLQQAQLYQMPIGNGDAdvatmvpstgsttaintisgvt 241
Cdd:cd21579   140 SSNGTTQALPEFTSVFSAPQS-AVNNVFIKQEMPSFDD----QQQGPLFQLLNSDLDQ---------------------- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 242 mstgsamlprhiqpggqvkhfqnvsqsqgnfnvtghfyPVPGLNLPPSPPNSQPGSPENQPELINTISPPPSYEATFGLK 321
Cdd:cd21579   193 --------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNLSPPPSYAASIASK 234

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1950476452 322 LVQSSQIPTLPNgLGTLSQGHIIMPTPKYNRRNNPELEKR 361
Cdd:cd21579   235 LAGQTPGLPPPG-VGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-H2C2_2 pfam13465
Zinc-finger double domain;
410-435 1.53e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 1950476452 410 ELTRHYRKHTGAKPFKCIACGRCFSR 435
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
271-448 5.83e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 271 NFNVTGHFYPVPGLNLPPSPPNSQPGSPENQPELINTISPPPSYEATFGLKLVQSSQIPTLPNGLGTLSQghiIMPTPKY 350
Cdd:COG5048   201 ENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS---QSSSPNE 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 351 NrrnNPELEKRRIHHCDYPGCTKVYTKSSHLKAHQRT--HTGE--KPYKCTWEGCDWRFARSDELTRHYRKHTGAKPFKC 426
Cdd:COG5048   278 S---DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE 354

                         170       180
                  ....*....|....*....|..
gi 1950476452 427 IACGRcfSRSDHLALHMKRHQN 448
Cdd:COG5048   355 KLLNS--SSKFSPLLNNEPPQS 374
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-407 4.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.21e-04
                          10        20
                  ....*....|....*....|....*...
gi 1950476452 380 HLKAHQRTHTGEKPYKCtwEGCDWRFAR 407
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
424-446 8.56e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 8.56e-03
                           10        20
                   ....*....|....*....|...
gi 1950476452  424 FKCIACGRCFSRSDHLALHMKRH 446
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
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 ...
 3-361 4.99e-123

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: 358.84  E-value: 4.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452   3 SSGLVLSTPN-LEESTVFTQLKPVRMSGESAEDTSVFEDiKPAIRILENQHDLAQltalrmeqrmpltmeARSEMDKYLS 81
Cdd:cd21579     1 AAGLRMSAGLaPGEEAVFTQLKPVLMSGGDGEESLLFGD-KPAVRGRSSPHDYNQ---------------TKSEMDKYLS 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452  82 SQLLPVPMVPDKKYRRESASVVDEFFSTEKPSstPYSVNINVILPDTTHLRTGLYRPAKPLTPFPQIKTEPGTSFtqpCS 161
Cdd:cd21579    65 PQPPPPPAPEDKKYRRESASVVDEFFSEDKGS--PYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPKHEPPPPTSF---CS 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 162 STAGSTQTLPDFTSVFSMPQSvAVNNIFIKQEMPSEIPlsgsLQQAQLYQMPIGNGDAdvatmvpstgsttaintisgvt 241
Cdd:cd21579   140 SSNGTTQALPEFTSVFSAPQS-AVNNVFIKQEMPSFDD----QQQGPLFQLLNSDLDQ---------------------- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 242 mstgsamlprhiqpggqvkhfqnvsqsqgnfnvtghfyPVPGLNLPPSPPNSQPGSPENQPELINTISPPPSYEATFGLK 321
Cdd:cd21579   193 --------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNLSPPPSYAASIASK 234

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1950476452 322 LVQSSQIPTLPNgLGTLSQGHIIMPTPKYNRRNNPELEKR 361
Cdd:cd21579   235 LAGQTPGLPPPG-VGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-H2C2_2 pfam13465
Zinc-finger double domain;
410-435 1.53e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 1950476452 410 ELTRHYRKHTGAKPFKCIACGRCFSR 435
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
271-448 5.83e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 271 NFNVTGHFYPVPGLNLPPSPPNSQPGSPENQPELINTISPPPSYEATFGLKLVQSSQIPTLPNGLGTLSQghiIMPTPKY 350
Cdd:COG5048   201 ENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS---QSSSPNE 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950476452 351 NrrnNPELEKRRIHHCDYPGCTKVYTKSSHLKAHQRT--HTGE--KPYKCTWEGCDWRFARSDELTRHYRKHTGAKPFKC 426
Cdd:COG5048   278 S---DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE 354

                         170       180
                  ....*....|....*....|..
gi 1950476452 427 IACGRcfSRSDHLALHMKRHQN 448
Cdd:COG5048   355 KLLNS--SSKFSPLLNNEPPQS 374
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-407 4.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.21e-04
                          10        20
                  ....*....|....*....|....*...
gi 1950476452 380 HLKAHQRTHTGEKPYKCtwEGCDWRFAR 407
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
346-424 6.47e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 6.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950476452 346 PTPKYNRRNNPELEKRRIHHCdyPGCTKVYTKSSHLKAHQRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 424
Cdd:COG5048    16 LSSTPKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-418 9.86e-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: 36.51  E-value: 9.86e-04
                          10        20
                  ....*....|....*....|....*
gi 1950476452 394 YKCTweGCDWRFARSDELTRHYRKH 418
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 424-446 1.24e-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: 36.12  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 1950476452 424 FKCIACGRCFSRSDHLALHMKRH 446
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
424-446 8.56e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 8.56e-03
                           10        20
                   ....*....|....*....|...
gi 1950476452  424 FKCIACGRCFSRSDHLALHMKRH 446
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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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