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Conserved domains on  [gi|568979886|ref|XP_006516048|]
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transcription factor Sp8 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 1-357 9.64e-143

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: 411.66  E-value: 9.64e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886   1 MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSSssgsCNVVGSSLSSFGVSGASRNGGsssaaaaaaaaaaaaa 80
Cdd:cd22538    1 MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSS----SSSLGSSLSGFGVSGSSRNGN---------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886  81 aLVSDSFSCGGSPGSSAFSLTSSSAAAAaaaaaaaasssPFANDYSVFQAPGVsggsggggggggggsgAHSQDSSHQPV 160
Cdd:cd22538   61 -LVSDSFSCNGSPGSSAFSLTSSTSSTS-----------PFANEYSVFQAPVS----------------SGSQEASHQPV 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 161 FISKVHTSVDGLQGIYPRVGMAHPYESWFKPSHPGLGAAAdvGSAGASSWWDVGAGWIDVQNPNGAAaLPGSLHPaaGGL 240
Cdd:cd22538  113 FISKVHTSVDSLQGIYPRVGMAHPYESWFKPSHPGIATGE--GGGGASSWWDVGAGWIDVQNPNGAA-LQTSLHS--GGL 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 241 QTSLHSPLGGYNSDYSGLSHSAFSSGASSHLLSPaGQHLMDGFKPVLPGSYPDSAPSPLAGAGSSMLSAGPAAQLGGSPR 320
Cdd:cd22538  188 QTSLHSPLGGYNSDYSGLGHSAFSTGASSHLLTT-GQHLMDGFKPVLPPSYPDSSPSPLAGAGGSMLTGGPTAPLGGSPR 266

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 568979886 321 SSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22538  267 SSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
zf-H2C2_2 pfam13465
Zinc-finger double domain;
402-425 3.19e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.19e-06
                          10        20
                  ....*....|....*....|....
gi 568979886  402 ELQRHLRTHTGEKRFACPVCNKRF 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-399 2.25e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.25e-04
                          10        20
                  ....*....|....*....|....*...
gi 568979886  372 HLKAHLRWHTGERPFVCNwlFCGKRFTR 399
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 ...
 416-438 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 568979886  416 FACPVCNKRFMRSDHLSKHVKTH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 1-357 9.64e-143

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: 411.66  E-value: 9.64e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886   1 MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSSssgsCNVVGSSLSSFGVSGASRNGGsssaaaaaaaaaaaaa 80
Cdd:cd22538    1 MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSS----SSSLGSSLSGFGVSGSSRNGN---------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886  81 aLVSDSFSCGGSPGSSAFSLTSSSAAAAaaaaaaaasssPFANDYSVFQAPGVsggsggggggggggsgAHSQDSSHQPV 160
Cdd:cd22538   61 -LVSDSFSCNGSPGSSAFSLTSSTSSTS-----------PFANEYSVFQAPVS----------------SGSQEASHQPV 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 161 FISKVHTSVDGLQGIYPRVGMAHPYESWFKPSHPGLGAAAdvGSAGASSWWDVGAGWIDVQNPNGAAaLPGSLHPaaGGL 240
Cdd:cd22538  113 FISKVHTSVDSLQGIYPRVGMAHPYESWFKPSHPGIATGE--GGGGASSWWDVGAGWIDVQNPNGAA-LQTSLHS--GGL 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 241 QTSLHSPLGGYNSDYSGLSHSAFSSGASSHLLSPaGQHLMDGFKPVLPGSYPDSAPSPLAGAGSSMLSAGPAAQLGGSPR 320
Cdd:cd22538  188 QTSLHSPLGGYNSDYSGLGHSAFSTGASSHLLTT-GQHLMDGFKPVLPPSYPDSSPSPLAGAGGSMLTGGPTAPLGGSPR 266

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 568979886 321 SSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22538  267 SSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
zf-H2C2_2 pfam13465
Zinc-finger double domain;
402-425 3.19e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.19e-06
                          10        20
                  ....*....|....*....|....
gi 568979886  402 ELQRHLRTHTGEKRFACPVCNKRF 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-399 2.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.25e-04
                          10        20
                  ....*....|....*....|....*...
gi 568979886  372 HLKAHLRWHTGERPFVCNwlFCGKRFTR 399
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 ...
 416-438 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 568979886  416 FACPVCNKRFMRSDHLSKHVKTH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 385-438 3.06e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.93  E-value: 3.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979886 385 PFVCNwlFCGKRFTRSDELQRHLRTHTGEKrfACPVCNKRFMRSDHLSKHV-KTH 438
Cdd:PHA00733  73 PYVCP--LCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKH 123
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
371-438 3.67e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 3.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979886 371 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACP--VCNKRFMRSDHLSKHVKTH 438
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQ 376
 
Name Accession Description Interval E-value
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 1-357 9.64e-143

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: 411.66  E-value: 9.64e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886   1 MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSSssgsCNVVGSSLSSFGVSGASRNGGsssaaaaaaaaaaaaa 80
Cdd:cd22538    1 MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSS----SSSLGSSLSGFGVSGSSRNGN---------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886  81 aLVSDSFSCGGSPGSSAFSLTSSSAAAAaaaaaaaasssPFANDYSVFQAPGVsggsggggggggggsgAHSQDSSHQPV 160
Cdd:cd22538   61 -LVSDSFSCNGSPGSSAFSLTSSTSSTS-----------PFANEYSVFQAPVS----------------SGSQEASHQPV 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 161 FISKVHTSVDGLQGIYPRVGMAHPYESWFKPSHPGLGAAAdvGSAGASSWWDVGAGWIDVQNPNGAAaLPGSLHPaaGGL 240
Cdd:cd22538  113 FISKVHTSVDSLQGIYPRVGMAHPYESWFKPSHPGIATGE--GGGGASSWWDVGAGWIDVQNPNGAA-LQTSLHS--GGL 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 241 QTSLHSPLGGYNSDYSGLSHSAFSSGASSHLLSPaGQHLMDGFKPVLPGSYPDSAPSPLAGAGSSMLSAGPAAQLGGSPR 320
Cdd:cd22538  188 QTSLHSPLGGYNSDYSGLGHSAFSTGASSHLLTT-GQHLMDGFKPVLPPSYPDSSPSPLAGAGGSMLTGGPTAPLGGSPR 266

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 568979886 321 SSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22538  267 SSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 1-357 5.10e-75

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: 237.96  E-value: 5.10e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886   1 MLAATCNKIGSPSPSPSSLSDSSssFGKG-FHPWKRSSSSssgsCNVvGSSLSSFGVSGASRNGGSSSAAAAaaaaaaaa 79
Cdd:cd22549    1 MLAATCNKIGNTSPLTTLPESSA--FAKGgFHPWKRSSSS----CNL-GSSLSGFAVATSRASGGLASGTGT-------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886  80 aalvSDSFSCGGSpgssafsltsssaaaaaaaaaAAASSSPFANDYS-VFQAPGVSggsggggggggggsgAHSQDSSHQ 158
Cdd:cd22549   66 ----ANSAFCLAS---------------------TSPTSSAFSSDYSgLFSNSTSV---------------ATPSQESGQ 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 159 PVFISKVHTSVDGLqgiYPRVGMAHPYESWFKPS-HPGLGAAAdvgSAGASSWWDVGAG---WIDVQNPngAAALPGSLH 234
Cdd:cd22549  106 SAFISKVHTSAESL---YPRVGMAHPYESWYKSGfHSTISGDV---SGGASSWWDVHTNpssWLEVQNP--AGGLQSSLH 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 235 paAGGLQTSLHSPLGGYNSDYSGLSHSAFSS----GASSHLLsPAGQHLM--DGFKPVLPgSYPDSapsPLAGAGSSMLS 308
Cdd:cd22549  178 --SGTPQASLHSQLGGYNPDFSSLTHSAFSStgisATASHLL-STSQHLLtqEGFKPVLP-SYTDS---SAANAMGSASI 250

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568979886 309 AGPAAQLGGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22549  251 ISGAATLGGGSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 180-357 3.46e-43

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: 150.09  E-value: 3.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 180 GMAHPYESWFKPSHPGLGAAADVGSAGASSWWDV--GAGWIDVqnpngaaalpgslhpaagglqtslhsplggynsdysg 257
Cdd:cd22543   37 DMAHPYESWFKPGHHATIAPGEVPSNEASSWWDVhpGGSWLDV------------------------------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 258 lshsafssgasSHLLSPAGQHLM--DGFKPVLPGSYPDSAPSPLagagssmlSAGPAAQLGGSPRSSARRYSGRATCDCP 335
Cdd:cd22543   80 -----------PHLLSPGGQHLLgqDGYKPVLPGASPESAGSDG--------SSLPGAASGGGSRRSARRYSGRATCDCP 140

                        170       180
                 ....*....|....*....|..
gi 568979886 336 NCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22543  141 NCQEAERLGPAGAGLRKKGLHS 162
SP6-9-like_N cd22547
N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to ...
 152-357 6.54e-35

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: 129.84  E-value: 6.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 152 SQDSSHQPVFISKVHTSVdglqGIYPRVGMAHPYESWFKP--SHPGLGAAADVGSAGASSWWDV---GAGWIDVqnpnga 226
Cdd:cd22547   36 VSSNSSQASLLQKVHSSV----SDSRPVYSHHPYESWPFNatSHHHKKEEVSSSANNSSSWWDMhsaAGSWLDE------ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 227 aalpgslHPAAGGLQTSlHSPLGGYNSDYSGLSHSAfssGASSHLLSPAGQHLMDGFKPVLPGSYPDSAPSPLAGAGSSM 306
Cdd:cd22547  106 -------SSAAATGPHS-QISPNYPSSDYSLGHLLA---SSSAPLLLSGQHLLQDTYKSMLPSQGDIGASSFPSSLLSQP 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979886 307 LSAGPAaqlggSPRSSaRRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22547  175 SLSGVP-----SPRSQ-RRYTGRATCDCPNCQEAERLGPAGAHLRKKNIHS 219
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 177-356 6.89e-27

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: 108.47  E-value: 6.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 177 PRVGMAHPYESWFKPSHPGLGAaadvGSAGASSWWDVGAG--WIDVQNPNGAAALPGSlhpaAGGLQTslhsPLGGYNSD 254
Cdd:cd22544   96 PPPDMAHPYESWFRPPHPGGSG----EEGGVPSWWDLHAGssWMDLQHGQGGLQSPGP----PGGLQP----PLGGYGSE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 255 YSglshsafSSGASSHLLsPAGQHLMdgfkpvlpgsypdsapSPLAGAGSSMLSAGPAAQLGGSPRSSAR---RYSGRAT 331
Cdd:cd22544  164 HQ-------LCGPPHHLL-PPAQHLM----------------GQEGPKLLEHPAEDPSLDGSPRPKGSRRsvpRSSGQAA 219

                        170       180
                 ....*....|....*....|....*
gi 568979886 332 CDCPNCQEAERLGPAGASLRRKGLH 356
Cdd:cd22544  220 CRCPNCQEAERLGPPPDGGKKKHLH 244
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 152-357 4.00e-26

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: 107.68  E-value: 4.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 152 SQDSShqpVFISKVHTSVDGLQGIYPRVGMAHPYESWFKPS-HPGLGAaadvGSAGA-SSWWDVGAGWIDVQNPNGAAAL 229
Cdd:cd22542  111 SQDPS---LLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGiHPGISS----SSTNAtASWWDMHSNTNWLSAQGQPDGL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979886 230 PGSLHPAAGglQTSLHSPLGGYNSDYSGL--SHSAFSSGASSHLLsPAGQHLM--DGFKPVLPgsypdsapsplagAGSS 305
Cdd:cd22542  184 QASLQPVPA--QTPLNPQLPSYTEFTTLNpaPYPAVGISSSSHLL-PSSQHMLsqDMYKPKPV-------------ANNG 247

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979886 306 MLSAGPAaqLGGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 357
Cdd:cd22542  248 LMEGGIG--LKSPSGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
402-425 3.19e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.19e-06
                          10        20
                  ....*....|....*....|....
gi 568979886  402 ELQRHLRTHTGEKRFACPVCNKRF 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-399 2.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.25e-04
                          10        20
                  ....*....|....*....|....*...
gi 568979886  372 HLKAHLRWHTGERPFVCNwlFCGKRFTR 399
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 ...
 386-410 8.43e-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: 8.43e-04
                          10        20
                  ....*....|....*....|....*
gi 568979886  386 FVCNwlFCGKRFTRSDELQRHLRTH 410
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 ...
 416-438 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 568979886  416 FACPVCNKRFMRSDHLSKHVKTH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 385-438 3.06e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.93  E-value: 3.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979886 385 PFVCNwlFCGKRFTRSDELQRHLRTHTGEKrfACPVCNKRFMRSDHLSKHV-KTH 438
Cdd:PHA00733  73 PYVCP--LCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKH 123
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
371-438 3.67e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 3.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979886 371 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACP--VCNKRFMRSDHLSKHVKTH 438
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQ 376
 
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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