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Conserved domains on  [gi|18858935|ref|NP_571798|]
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Krueppel-like factor 17 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 6-326 5.54e-144

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; 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 N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


:

Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 412.90  E-value: 5.54e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935   6 AMLPSINTFSNNHILDEKQSEIVRDWKVDIAKTNPRAGDVRPLIEVEFSIVESPPLAKDEDDLSKFLDLEFILSNTVTSD 85
Cdd:cd22056   1 AMLPSISTFASLQPLEEKQPEILCRWSVDAASSEVEFSIVQSPIEVPKDDDELGKFLDEEDILSNFLDLEFILSSSNGSS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  86 NDNTSAPPPAYSLPESPESCSTVYDSDGC-HPTPNAYCGTNFNSRPGHSLVAELFTPDMNYQGE---YNLKGHLDRLEYT 161
Cdd:cd22056  81 SGPSQQQQCAYPLPESPESCSTGSDSDGSdAPQPYHGSAGFTSSSPVHSLMAELLTPEMNYPGEsspDSAGKARDGREYT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 162 ELRALNTRNQ--QHLTNSNNAGYKIKTENQEQSCMMVNDYMGHYYAQEPQRVMQHQTYGHHVQQDV-------PRDILGR 232
Cdd:cd22056 161 ELRALPTAPPahQPATSPPPLGYKIKTEPVEQSCMMAAGGGGFMGQQKPKHQMHSVHPQAFTHHQAagpgalqGRGGRGG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 233 KDCILTEMNTQHHIDISHQQQFiNNAHFPPQYAQH--QQYHGHFNMFSEPLRANHPAMPGVMLTPPSSPLL----GFLSP 306
Cdd:cd22056 241 PDCHLLHSSHHHHHHHHLQYQY-MNAPYPPHYAHQgaPQFHGQYSVFREPMRVHHQGHPGSMLTPPSSPPLlefyAQDEP 319

                       330       340
                ....*....|....*....|
gi 18858935 307 EDSKPKRGRRSWARKRTATH 326
Cdd:cd22056 320 EDIKPKRGRRSWARKRTATH 339
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-397 3.23e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.23e-04
                          10        20
                  ....*....|....*....|....*.
gi 18858935   372 ELTRHYRKHTGHRPFQCHLCERAFSR 397
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 326-350 4.60e-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: 34.20  E-value: 4.60e-03
                          10        20
                  ....*....|....*....|....*
gi 18858935   326 HSCefPGCGKTYTKSSHLKAHMRTH 350
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-369 8.32e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.32e-03
                          10        20
                  ....*....|....*....|....*...
gi 18858935   342 HLKAHMRTHTGEKPYHCswEGCGWKFAR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
 
Name Accession Description Interval E-value
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 6-326 5.54e-144

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; 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 N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 412.90  E-value: 5.54e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935   6 AMLPSINTFSNNHILDEKQSEIVRDWKVDIAKTNPRAGDVRPLIEVEFSIVESPPLAKDEDDLSKFLDLEFILSNTVTSD 85
Cdd:cd22056   1 AMLPSISTFASLQPLEEKQPEILCRWSVDAASSEVEFSIVQSPIEVPKDDDELGKFLDEEDILSNFLDLEFILSSSNGSS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  86 NDNTSAPPPAYSLPESPESCSTVYDSDGC-HPTPNAYCGTNFNSRPGHSLVAELFTPDMNYQGE---YNLKGHLDRLEYT 161
Cdd:cd22056  81 SGPSQQQQCAYPLPESPESCSTGSDSDGSdAPQPYHGSAGFTSSSPVHSLMAELLTPEMNYPGEsspDSAGKARDGREYT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 162 ELRALNTRNQ--QHLTNSNNAGYKIKTENQEQSCMMVNDYMGHYYAQEPQRVMQHQTYGHHVQQDV-------PRDILGR 232
Cdd:cd22056 161 ELRALPTAPPahQPATSPPPLGYKIKTEPVEQSCMMAAGGGGFMGQQKPKHQMHSVHPQAFTHHQAagpgalqGRGGRGG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 233 KDCILTEMNTQHHIDISHQQQFiNNAHFPPQYAQH--QQYHGHFNMFSEPLRANHPAMPGVMLTPPSSPLL----GFLSP 306
Cdd:cd22056 241 PDCHLLHSSHHHHHHHHLQYQY-MNAPYPPHYAHQgaPQFHGQYSVFREPMRVHHQGHPGSMLTPPSSPPLlefyAQDEP 319

                       330       340
                ....*....|....*....|
gi 18858935 307 EDSKPKRGRRSWARKRTATH 326
Cdd:cd22056 320 EDIKPKRGRRSWARKRTATH 339
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-397 3.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.23e-04
                          10        20
                  ....*....|....*....|....*.
gi 18858935   372 ELTRHYRKHTGHRPFQCHLCERAFSR 397
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-393 1.86e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 248 ISHQQQFINNAHFPPQYAQHQQY---HGHFNMfSEPLRANHPAMPGVMLTPPSSPLlgflspedSKPKRGRRSWARK--- 321
Cdd:COG5048 211 IPSSSSDQNLENSSSSLPLTTNSqlsPKSLLS-QSPSSLSSSDSSSSASESPRSSL--------PTASSQSSSPNESdss 281

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858935 322 --RTATHSCEFPGCGKTYTKSSHLKAHMRT--HTGE--KPYHCSWEGCGWKFARSDELTRHYRKHTGHRPFQCHLCER 393
Cdd:COG5048 282 seKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNS 359
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 326-350 4.60e-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: 34.20  E-value: 4.60e-03
                          10        20
                  ....*....|....*....|....*
gi 18858935   326 HSCefPGCGKTYTKSSHLKAHMRTH 350
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-369 8.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.32e-03
                          10        20
                  ....*....|....*....|....*...
gi 18858935   342 HLKAHMRTHTGEKPYHCswEGCGWKFAR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
 
Name Accession Description Interval E-value
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 6-326 5.54e-144

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; 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 N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 412.90  E-value: 5.54e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935   6 AMLPSINTFSNNHILDEKQSEIVRDWKVDIAKTNPRAGDVRPLIEVEFSIVESPPLAKDEDDLSKFLDLEFILSNTVTSD 85
Cdd:cd22056   1 AMLPSISTFASLQPLEEKQPEILCRWSVDAASSEVEFSIVQSPIEVPKDDDELGKFLDEEDILSNFLDLEFILSSSNGSS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  86 NDNTSAPPPAYSLPESPESCSTVYDSDGC-HPTPNAYCGTNFNSRPGHSLVAELFTPDMNYQGE---YNLKGHLDRLEYT 161
Cdd:cd22056  81 SGPSQQQQCAYPLPESPESCSTGSDSDGSdAPQPYHGSAGFTSSSPVHSLMAELLTPEMNYPGEsspDSAGKARDGREYT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 162 ELRALNTRNQ--QHLTNSNNAGYKIKTENQEQSCMMVNDYMGHYYAQEPQRVMQHQTYGHHVQQDV-------PRDILGR 232
Cdd:cd22056 161 ELRALPTAPPahQPATSPPPLGYKIKTEPVEQSCMMAAGGGGFMGQQKPKHQMHSVHPQAFTHHQAagpgalqGRGGRGG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 233 KDCILTEMNTQHHIDISHQQQFiNNAHFPPQYAQH--QQYHGHFNMFSEPLRANHPAMPGVMLTPPSSPLL----GFLSP 306
Cdd:cd22056 241 PDCHLLHSSHHHHHHHHLQYQY-MNAPYPPHYAHQgaPQFHGQYSVFREPMRVHHQGHPGSMLTPPSSPPLlefyAQDEP 319

                       330       340
                ....*....|....*....|
gi 18858935 307 EDSKPKRGRRSWARKRTATH 326
Cdd:cd22056 320 EDIKPKRGRRSWARKRTATH 339
KLF1_2_4_N cd21972
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ...
 51-326 2.34e-83

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: 253.37  E-value: 2.34e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  51 VEFSIVESPPLAKDEDDLSKFLDLEFILSNTVTSDNDNTSAPPPAYSLPESPESCSTVYDSDGCHPTPNAYCGTNFNSRP 130
Cdd:cd21972   1 SESSLVSSGPFAKPEDDLSKFLDLEFILSNTVTSDNDNPPPPDPAYPPPESPESCSTVYDSDGCHPTPNAYCGPNGPGLP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 131 GHSLVAelftpdmnyqgeynlkghldrleytelralntrnqqhlTNSNNAGYKIKTENQEQSCMMVNDYMGHYYAQEPQR 210
Cdd:cd21972  81 GHFLLA--------------------------------------GNSPNLGPKIKTENQEQACMPVAGYSGHYGPREPQR 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 211 VMQHqtyghhvqqdvprdilgrkdciltemntqhhidishqqqfinnaHFPPQYAQHQQYHGHFNMFSEPLRANHPAMPG 290
Cdd:cd21972 123 VPPA--------------------------------------------PPPPQYAGHFQYHGHFNMFSPPLRANHPGMST 158

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 18858935 291 VMLTPPSSPLLGFLSPEDSKPKRGRRSWARKRTATH 326
Cdd:cd21972 159 VMLTPLSTPPLGFLSPEEAKPKRGRRSWARKRTATH 194
KLF2_N cd21583
N-terminal domain of Kruppel-like factor 2; Kruppel-like Factor 2 (KLF2, also known as ...
 7-326 5.48e-43

N-terminal domain of Kruppel-like factor 2; Kruppel-like Factor 2 (KLF2, also known as Krueppel-like factor 2 or lung Kruppel-like Factor/LKLF) is a protein that, in humans, is encoded by the KLF2 gene on chromosome 19. It has been implicated in a variety of biochemical processes in the human body, including lung development, embryonic erythropoiesis, epithelial integrity, T-cell viability, and adipogenesis. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF2 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 KLF2, which is related to the N-terminal domains of KLF1 and KLF4.


Pssm-ID: 409229 [Multi-domain]  Cd Length: 299  Bit Score: 152.11  E-value: 5.48e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935   7 MLPSINTFSNNhilDEKQSEivRDWKVDIAKTNPRAGDVRPlievefSIVESPPLAKDEDDLSKFLDLEFILSNTVTSDN 86
Cdd:cd21583   4 ILPSISTFANQ---KEKCWE--DRWKGEEDKSSLSSCLLDL------QNGDSCLGRKDDEDLDNYLDLDFILANTAGSDS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  87 DNTSAPPPAYSLPESPESCSTvydsdgcHPTPNAYCGTNFNSRP---GHSLVAELFTPDMNYQGEYN-LKGHLdrleytE 162
Cdd:cd21583  73 AGAAGGGYYGSLPEPAAPYSA-------SNPPGAYSVPEQGSPPppySSSLMAELLRDSDSDYGPSNsIQGRF------L 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 163 LRALNTRNQQHLTN----SNNAGY------------KIKTENqEQSCMMvndymghyyAQEPQRVmqhqtyGHHVQQDV- 225
Cdd:cd21583 140 VSSAFFPRQDDPDSikvePSMDSYgpvmgmvpqscpKIKQEG-NVSCMM---------SFEQPRL------ANSPQAAGs 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 226 -----PRDILGRKDCiLTEMNTQHHIDISHQQQFinnaHFPPQYAQHQQYHGHFNMFSEPLRANHPAmPGVMLTPPSSPL 300
Cdd:cd21583 204 mtpplSPDDLMASEC-QQQMMCSPSFPQPHHPHY----PPPPQPPLQYQSPHQFGLFEDGLPLQPSA-QRVLLTPPSSPL 277

                       330       340
                ....*....|....*....|....*.
gi 18858935 301 LgflsPEDSKPKRGRRSWARKRTATH 326
Cdd:cd21583 278 E----LLESKPKRGRRSWPRKRTATH 299
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 1-326 1.52e-20

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 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 KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 91.68  E-value: 1.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935   1 MALADAMLPSINTFSNNHILDEK---QSEIVRDWKVDIAKTN---PRAGDVRPLIEVefsiveSPPLAKDEDDLSKFLDL 74
Cdd:cd21582   4 MALSGTLLPSISTFASGPAVKEKalgQGSANNRWREELSHLKrpcPPLGGRCYDQDP------PLGMRRKEEEFNDLLDY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  75 EFILSNTV------------TSDNDNTSAPPPA-YSLP-ESPESCSTVYdsdgchPTPNAYCGTNFNSRPGHSLVAELFT 140
Cdd:cd21582  78 DFILSNSLlqqqqqqqqaasTSSSTSSSSSSPYsYQLPsPQGTATSFLY------PIPRANLADINDVSPSGGFVAELMR 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 141 PDM--------NYQGEYNLKGHLDRLEYtelralntrNQQHLTNSNNAGY---------------KIKTENqEQSCMMVN 197
Cdd:cd21582 152 PDLdpaylqptSLHGKFVVKTTMDMGDY---------SQSINVSKSAPMTkssvapssslpfmcpRIKQEN-PSTCTISR 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 198 DYMGHYYAQEPQ-----RVMQHQTYGH----HVQQDVPRDILGRKDCILTEmnTQHHIDISHQQQFINNA---HFPPQYA 265
Cdd:cd21582 222 PMDGHLGGNSQHgfsqrAPLPSRTTPSggpgGGNSSTAESLMSRDHHPSSQ--VLSHPPLPLPQGYHPSPgypPFPPPPS 299

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18858935 266 QHQQYHghfnmfseplranhpampgvMLTPPSSPLlgflsPEDSKPKRGRRSWARKRTATH 326
Cdd:cd21582 300 QPQQYQ--------------------ELMSPGSCL-----PEEPKPKRGRRSWPRKRTATH 335
KLF1_N cd21581
N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as ...
 6-326 4.35e-09

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: 56.98  E-value: 4.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935   6 AMLPSintFSNNHILDeKQSEIVRDWKVDIAKTN-PRAGDVRPLIEVEFSIVESPP-LAKDEDDLSKFLDLEFILSN--- 80
Cdd:cd21581   1 AVLPS---FSSFSFLD-HQSDNMKVWKSEEGQLPlDGPPDKLSPSGSEQLQVSQPMtEELLDDDSQASWDIEFLLSNwss 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935  81 -TVTSDNDNTSAPPPAYSLPESPESCSTVYDSDGCHPTPNAYcgtnfnsrpghSLVAELFTPD--MNYQGEYNLKGHLD- 156
Cdd:cd21581  77 pSLNPSLDNNTQALPQEEQPGAYYEPPKKDQPGTEGLQVGGP-----------GLMAELLSPEesTGWAPPEPHHGYPDa 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 157 ---RLEYTELRALNTRNQQHLTNSNNAGYKIKTENQEqscmmvndyMGHYYAQEPQRVM--------QHQTYghhvqQDV 225
Cdd:cd21581 146 fvgPALFPAPANVDQFGFPQGGSVDRRGNLSKSGSWD---------FGSYYPQQHPSVVafpdsrfgPLSGP-----QAL 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 226 PRDilgrkdciltemnTQHHidiSHQQQFINNAHFPPQYAQHQQYHGHfnmfseplranhPAMPGVMLTPPSSPllgfls 305
Cdd:cd21581 212 TPD-------------PQHY---GYFQLFRHNAALFPDYAHSPGPGHL------------PLGQQPLLPDPPLP------ 257

                       330       340
                ....*....|....*....|.
gi 18858935 306 PEDSKPKRGRRSWARKRTATH 326
Cdd:cd21581 258 PGGAEGKRGRRSWAKKRPAVH 278
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-397 3.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.23e-04
                          10        20
                  ....*....|....*....|....*.
gi 18858935   372 ELTRHYRKHTGHRPFQCHLCERAFSR 397
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 386-408 1.16e-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: 1.16e-03
                          10        20
                  ....*....|....*....|...
gi 18858935   386 FQCHLCERAFSRSDHLALHMKRH 408
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-393 1.86e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858935 248 ISHQQQFINNAHFPPQYAQHQQY---HGHFNMfSEPLRANHPAMPGVMLTPPSSPLlgflspedSKPKRGRRSWARK--- 321
Cdd:COG5048 211 IPSSSSDQNLENSSSSLPLTTNSqlsPKSLLS-QSPSSLSSSDSSSSASESPRSSL--------PTASSQSSSPNESdss 281

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858935 322 --RTATHSCEFPGCGKTYTKSSHLKAHMRT--HTGE--KPYHCSWEGCGWKFARSDELTRHYRKHTGHRPFQCHLCER 393
Cdd:COG5048 282 seKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNS 359
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 326-350 4.60e-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: 34.20  E-value: 4.60e-03
                          10        20
                  ....*....|....*....|....*
gi 18858935   326 HSCefPGCGKTYTKSSHLKAHMRTH 350
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-369 8.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.32e-03
                          10        20
                  ....*....|....*....|....*...
gi 18858935   342 HLKAHMRTHTGEKPYHCswEGCGWKFAR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
 
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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