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Conserved domains on  [gi|47086307|ref|NP_998028|]
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transcription factor Sp7 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 2-301 3.40e-147

N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP7, also called Osterix (Osx) in humans, is highly conserved among bone-forming vertebrates. It plays a major role, along with Runx2 and Dlx5 in driving the differentiation of mesenchymal precursor cells into osteoblasts and eventually osteocytes. SP7 also plays a regulatory role by inhibiting chondrocyte differentiation, maintaining the balance between differentiation of mesenchymal precursor cells into ossified bone or cartilage. Mutations of this gene have been associated with multiple dysfunctional bone phenotypes in vertebrates. SP7 is thought to play a role in diseases such as Osteogenesis imperfecta. SP7 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP7.


:

Pssm-ID: 411691 [Multi-domain]  Cd Length: 297  Bit Score: 420.84  E-value: 3.40e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307   2 AASILEEETRYGSSPLAMLTATCNKFGSTSPVRDSATPGKPGSTiPIKKAYSMTSELQSAKNGRNESVADSYTGSFSSSG 81
Cdd:cd22542   1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGNN-PGKKPYSLGSDLSSAKSRSSELMGDSYTATFSSGN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  82 GLLTPTGSPPPAptGAYGSEYNPFS-TFQTSSVSQDPSLLGSKA--TADCLTSVNTYLDMTHPYGSWYK-GIHPGITASP 157
Cdd:cd22542  80 GLMSPSGSPQAS--TTYGNDYNPFShSFPTSSGSQDPSLLVSKGhpSADCLPSVYTSLDMAHPYGSWYKtGIHPGISSSS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 158 ANATSSWWDVHTNANWLSPgQAQPDSLQAPLQPVAPQASLNPQMPSYTpDFTPLNPAPYPSVGLSSSSHLLQSSQHMLPQ 237
Cdd:cd22542 158 TNATASWWDMHSNTNWLSA-QGQPDGLQASLQPVPAQTPLNPQLPSYT-EFTTLNPAPYPAVGISSSSHLLPSSQHMLSQ 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086307 238 DMYKPKPVPTSGILDNSMGLKSarGSGYAAGSTTGRSSCDCPNCQELERLGASAASLRKKPVHS 301
Cdd:cd22542 236 DMYKPKPVANNGLMEGGIGLKS--PSGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
346-371 5.02e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 5.02e-06
                          10        20
                  ....*....|....*....|....*.
gi 47086307   346 ELERHVRTHTREKKFTCLLCNKRFTR 371
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-343 1.55e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.55e-05
                          10        20
                  ....*....|....*....|....*...
gi 47086307   316 HLKAHLRWHTGERPFVCNwlFCGKRFTR 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 300-324 3.43e-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: 34.97  E-value: 3.43e-03
                          10        20
                  ....*....|....*....|....*
gi 47086307   300 HSCHIpgCGKVYGKASHLKAHLRWH 324
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 2-301 3.40e-147

N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP7, also called Osterix (Osx) in humans, is highly conserved among bone-forming vertebrates. It plays a major role, along with Runx2 and Dlx5 in driving the differentiation of mesenchymal precursor cells into osteoblasts and eventually osteocytes. SP7 also plays a regulatory role by inhibiting chondrocyte differentiation, maintaining the balance between differentiation of mesenchymal precursor cells into ossified bone or cartilage. Mutations of this gene have been associated with multiple dysfunctional bone phenotypes in vertebrates. SP7 is thought to play a role in diseases such as Osteogenesis imperfecta. SP7 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP7.


Pssm-ID: 411691 [Multi-domain]  Cd Length: 297  Bit Score: 420.84  E-value: 3.40e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307   2 AASILEEETRYGSSPLAMLTATCNKFGSTSPVRDSATPGKPGSTiPIKKAYSMTSELQSAKNGRNESVADSYTGSFSSSG 81
Cdd:cd22542   1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGNN-PGKKPYSLGSDLSSAKSRSSELMGDSYTATFSSGN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  82 GLLTPTGSPPPAptGAYGSEYNPFS-TFQTSSVSQDPSLLGSKA--TADCLTSVNTYLDMTHPYGSWYK-GIHPGITASP 157
Cdd:cd22542  80 GLMSPSGSPQAS--TTYGNDYNPFShSFPTSSGSQDPSLLVSKGhpSADCLPSVYTSLDMAHPYGSWYKtGIHPGISSSS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 158 ANATSSWWDVHTNANWLSPgQAQPDSLQAPLQPVAPQASLNPQMPSYTpDFTPLNPAPYPSVGLSSSSHLLQSSQHMLPQ 237
Cdd:cd22542 158 TNATASWWDMHSNTNWLSA-QGQPDGLQASLQPVPAQTPLNPQLPSYT-EFTTLNPAPYPAVGISSSSHLLPSSQHMLSQ 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086307 238 DMYKPKPVPTSGILDNSMGLKSarGSGYAAGSTTGRSSCDCPNCQELERLGASAASLRKKPVHS 301
Cdd:cd22542 236 DMYKPKPVANNGLMEGGIGLKS--PSGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
346-371 5.02e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 5.02e-06
                          10        20
                  ....*....|....*....|....*.
gi 47086307   346 ELERHVRTHTREKKFTCLLCNKRFTR 371
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-343 1.55e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.55e-05
                          10        20
                  ....*....|....*....|....*...
gi 47086307   316 HLKAHLRWHTGERPFVCNwlFCGKRFTR 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
360-382 2.13e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|...
gi 47086307    360 FTCLLCNKRFTRSDHLSKHQKTH 382
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
330-354 3.34e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 3.34e-03
                           10        20
                   ....*....|....*....|....*
gi 47086307    330 FVCNWlfCGKRFTRSDELERHVRTH 354
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 300-324 3.43e-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: 34.97  E-value: 3.43e-03
                          10        20
                  ....*....|....*....|....*
gi 47086307   300 HSCHIpgCGKVYGKASHLKAHLRWH 324
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 2-301 3.40e-147

N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP7, also called Osterix (Osx) in humans, is highly conserved among bone-forming vertebrates. It plays a major role, along with Runx2 and Dlx5 in driving the differentiation of mesenchymal precursor cells into osteoblasts and eventually osteocytes. SP7 also plays a regulatory role by inhibiting chondrocyte differentiation, maintaining the balance between differentiation of mesenchymal precursor cells into ossified bone or cartilage. Mutations of this gene have been associated with multiple dysfunctional bone phenotypes in vertebrates. SP7 is thought to play a role in diseases such as Osteogenesis imperfecta. SP7 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP7.


Pssm-ID: 411691 [Multi-domain]  Cd Length: 297  Bit Score: 420.84  E-value: 3.40e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307   2 AASILEEETRYGSSPLAMLTATCNKFGSTSPVRDSATPGKPGSTiPIKKAYSMTSELQSAKNGRNESVADSYTGSFSSSG 81
Cdd:cd22542   1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGNN-PGKKPYSLGSDLSSAKSRSSELMGDSYTATFSSGN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  82 GLLTPTGSPPPAptGAYGSEYNPFS-TFQTSSVSQDPSLLGSKA--TADCLTSVNTYLDMTHPYGSWYK-GIHPGITASP 157
Cdd:cd22542  80 GLMSPSGSPQAS--TTYGNDYNPFShSFPTSSGSQDPSLLVSKGhpSADCLPSVYTSLDMAHPYGSWYKtGIHPGISSSS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 158 ANATSSWWDVHTNANWLSPgQAQPDSLQAPLQPVAPQASLNPQMPSYTpDFTPLNPAPYPSVGLSSSSHLLQSSQHMLPQ 237
Cdd:cd22542 158 TNATASWWDMHSNTNWLSA-QGQPDGLQASLQPVPAQTPLNPQLPSYT-EFTTLNPAPYPAVGISSSSHLLPSSQHMLSQ 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086307 238 DMYKPKPVPTSGILDNSMGLKSarGSGYAAGSTTGRSSCDCPNCQELERLGASAASLRKKPVHS 301
Cdd:cd22542 236 DMYKPKPVANNGLMEGGIGLKS--PSGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 19-301 6.16e-38

N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP9 plays a role in limb outgrowth. It is expressed during embryogenesis in the forming apical ectodermal ridge, restricted regions of the central nervous system, and tail bud. SP8 and SP9 are two closely related transcription factors that mediate FGF10 signaling, which in turn regulates FGF8 expression which is essential for normal limb development. Both SP8 and SP9 have been found in vertebrates, but only SP8 is present in invertebrates. SP9 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP9.


Pssm-ID: 411695 [Multi-domain]  Cd Length: 299  Bit Score: 139.74  E-value: 6.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  19 MLTATCNKFGSTSPVR---DSATPGKpGSTIPIKKAYSMTSELQS----AKNGRNESVADSYTGSFSSSGGLLTPTGSPP 91
Cdd:cd22549   1 MLAATCNKIGNTSPLTtlpESSAFAK-GGFHPWKRSSSSCNLGSSlsgfAVATSRASGGLASGTGTANSAFCLASTSPTS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  92 PAPTGAYGSEYNPFSTFQTSSVSQDPSLLGSK--ATADCLTSvntYLDMTHPYGSWYK-GIHPGITASPANATSSWWDVH 168
Cdd:cd22549  80 SAFSSDYSGLFSNSTSVATPSQESGQSAFISKvhTSAESLYP---RVGMAHPYESWYKsGFHSTISGDVSGGASSWWDVH 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 169 TN-ANWLSPgQAQPDSLQAPLQPVAPQASLNPQMPSYTPDFTPLNPAPYPSVGLSSSSHLL-QSSQHMLPQDMYKP---- 242
Cdd:cd22549 157 TNpSSWLEV-QNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFSSTGISATASHLlSTSQHLLTQEGFKPvlps 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086307 243 ---KPVPTSGILDNSMGLKSARGSGYAAGST--TGRSSCDCPNCQELERLGASAASLRKKPVHS 301
Cdd:cd22549 236 ytdSSAANAMGSASIISGAATLGGGSARSARrySGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 19-301 1.14e-27

N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP8 is crucial for limb outgrowth and neuropore closure. It is expressed during embryogenesis in the forming apical ectodermal ridge, restricted regions of the central nervous system, and tail bud. SP8 and SP9 are two closely related transcription factors that mediate FGF10 signaling, which in turn regulates FGF8 expression which is essential for normal limb development. Both SP8 and SP9 have been found in vertebrates, but only SP8 is present in invertebrates. SP8 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP8.


Pssm-ID: 411690 [Multi-domain]  Cd Length: 303  Bit Score: 111.59  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  19 MLTATCNKFGSTSP----VRDSATPGKPGSTiPIKKAYSMTSELQSAKNG-------RNES-VADSYT--GSFSSSGGLL 84
Cdd:cd22538   1 MLAATCNKIGSPSPspssLSDSSSSFGKGFH-PWKRSSSSSSSLGSSLSGfgvsgssRNGNlVSDSFScnGSPGSSAFSL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  85 TPTGSPppapTGAYGSEYNPFSTFQTSSVSQDP--SLLGSK--ATADCLTSVNTYLDMTHPYGSWYKGIHPGITASPANA 160
Cdd:cd22538  80 TSSTSS----TSPFANEYSVFQAPVSSGSQEAShqPVFISKvhTSVDSLQGIYPRVGMAHPYESWFKPSHPGIATGEGGG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 161 T-SSWWDVHtnANWLSPGQAQPDSLQAPLQPVAPQASLNPQMPSYTPDFTPLNPAPYPSVGLSSSSHLLQSS----QHML 235
Cdd:cd22538 156 GaSSWWDVG--AGWIDVQNPNGAALQTSLHSGGLQTSLHSPLGGYNSDYSGLGHSAFSTGASSHLLTTGQHLmdgfKPVL 233

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 236 PQDMYKPKPVPTSGILDNSMGLKSARGSGYAAGST----TGRSSCDCPNCQELERLGASAASLRKKPVHS 301
Cdd:cd22538 234 PPSYPDSSPSPLAGAGGSMLTGGPTAPLGGSPRSSarrySGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 136-301 1.17e-26

N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the related N-terminal domains of SP6-SP9, and similar proteins.


Pssm-ID: 411692  Cd Length: 162  Bit Score: 105.02  E-value: 1.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 136 LDMTHPYGSWYKGIHPGITAS---PANATSSWWDVHTNANWLSpgqaQPDSLQAPLQPVAPQASLNPQMPSYTPDFTPLN 212
Cdd:cd22543  36 LDMAHPYESWFKPGHHATIAPgevPSNEASSWWDVHPGGSWLD----VPHLLSPGGQHLLGQDGYKPVLPGASPESAGSD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 213 PApypsvglsssshllqssqhmlpqdmyKPKPVPTSGildnsmglksarGSGYAAGSTTGRSSCDCPNCQELERLGASAA 292
Cdd:cd22543 112 GS--------------------------SLPGAASGG------------GSRRSARRYSGRATCDCPNCQEAERLGPAGA 153


                ....*....
gi 47086307 293 SLRKKPVHS 301
Cdd:cd22543 154 GLRKKGLHS 162
SP6-9-like_N cd22547
N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to ...
 87-301 6.44e-22

N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to SP6, SP8 and SP9; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP6, also known as epiprofin, shows specific expression pattern in hair follicles and the apical ectodermal ridge (AER) of the developing limbs. SP6 null mice are nude and show defects in skin, teeth, limbs (syndactyly and oligodactyly), and lung alveoli. SP9 plays a role in limb outgrowth. It is expressed during embryogenesis in the forming AER, restricted regions of the central nervous system, and tail bud. SP8 and SP9 are two closely related transcription factors that mediate FGF10 signaling, which in turn regulates FGF8 expression which is essential for normal limb development. Both SP8 and SP9 have been found in vertebrates, but only SP8 is present in invertebrates. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of invertebrate SPs similar to SP6, SP8, and SP9.


Pssm-ID: 411694  Cd Length: 219  Bit Score: 93.63  E-value: 6.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  87 TGSPPPAPTGAYGSEYNPF-STFQTSSVSQDPSLLGSKATADCLTSVNTYldMTHPYGSWYKG-----IHPGITASPANA 160
Cdd:cd22547  11 SKSPPPLADAAVGKGFHPWkKSPPSVSSNSSQASLLQKVHSSVSDSRPVY--SHHPYESWPFNatshhHKKEEVSSSANN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 161 TSSWWDVHTNA-NWLSPGQAQPDSLQAPLQPVAPQA--SLNPQMPSYTPDFtpLNPAPYpsvglsssshllqssqhmLPQ 237
Cdd:cd22547  89 SSSWWDMHSAAgSWLDESSAAATGPHSQISPNYPSSdySLGHLLASSSAPL--LLSGQH------------------LLQ 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086307 238 DMYK-PKPVPTSGILDNSMGLKSARGSGYAAGST------TGRSSCDCPNCQELERLGASAASLRKKPVHS 301
Cdd:cd22547 149 DTYKsMLPSQGDIGASSFPSSLLSQPSLSGVPSPrsqrryTGRATCDCPNCQEAERLGPAGAHLRKKNIHS 219
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 19-300 6.64e-19

N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP6, also known as epiprofin, shows specific expression pattern in hair follicles and the apical ectodermal ridge (AER) of the developing limbs. SP6 null mice are nude and show defects in skin, teeth, limbs (syndactyly and oligodactyly), and lung alveoli. SP6 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP6.


Pssm-ID: 411693 [Multi-domain]  Cd Length: 245  Bit Score: 85.74  E-value: 6.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  19 MLTATCNKFGSTSPvrdSATPGKPGstipikkaysmTSELQSAKNGRNESVADSY-TGSFSSSGGLLTPTGSPPPAPTGA 97
Cdd:cd22544   1 MLTAVCGSLGNQHS---ETPRASPP-----------TLDLQPLQPYQIHSSPEAGdYPSPLQPTELQSLPLGPGVDFSAR 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307  98 YGSEYNPFSTFQTSSVSQDPSLLGSKatadcltSVNTYLDMTHPYGSWYKGIHPGITASPAnATSSWWDVHTNANW--LS 175
Cdd:cd22544  67 ESYEPHSSRRTCLDLESDLPLGPFPK-------LLHPPPDMAHPYESWFRPPHPGGSGEEG-GVPSWWDLHAGSSWmdLQ 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086307 176 PGQAqpdSLQAPlqpvAPQASLNPQMPSYTPDFTPLNPAPYpsvglssssHLLQSSQHMLPQDMYKPKPVPTSGILDNSM 255
Cdd:cd22544 139 HGQG---GLQSP----GPPGGLQPPLGGYGSEHQLCGPPHH---------LLPPAQHLMGQEGPKLLEHPAEDPSLDGSP 202

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 47086307 256 GLKSARGSgyaAGSTTGRSSCDCPNCQELERLGASAASLRKKPVH 300
Cdd:cd22544 203 RPKGSRRS---VPRSSGQAACRCPNCQEAERLGPPPDGGKKKHLH 244
zf-H2C2_2 pfam13465
Zinc-finger double domain;
346-371 5.02e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 5.02e-06
                          10        20
                  ....*....|....*....|....*.
gi 47086307   346 ELERHVRTHTREKKFTCLLCNKRFTR 371
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 360-382 1.13e-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: 41.90  E-value: 1.13e-05
                          10        20
                  ....*....|....*....|...
gi 47086307   360 FTCLLCNKRFTRSDHLSKHQKTH 382
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-343 1.55e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.55e-05
                          10        20
                  ....*....|....*....|....*...
gi 47086307   316 HLKAHLRWHTGERPFVCNwlFCGKRFTR 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-354 9.97e-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: 39.21  E-value: 9.97e-05
                          10        20
                  ....*....|....*....|....*
gi 47086307   330 FVCNwlFCGKRFTRSDELERHVRTH 354
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
360-382 2.13e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|...
gi 47086307    360 FTCLLCNKRFTRSDHLSKHQKTH 382
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
330-354 3.34e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 3.34e-03
                           10        20
                   ....*....|....*....|....*
gi 47086307    330 FVCNWlfCGKRFTRSDELERHVRTH 354
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 300-324 3.43e-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: 34.97  E-value: 3.43e-03
                          10        20
                  ....*....|....*....|....*
gi 47086307   300 HSCHIpgCGKVYGKASHLKAHLRWH 324
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 360-382 4.83e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 4.83e-03
                          10        20
                  ....*....|....*....|...
gi 47086307   360 FTCLLCNKRFTRSDHLSKHQKTH 382
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 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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