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Conserved domains on  [gi|223646113|ref|NP_001138722|]
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transcription factor Sp9 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 19-333 1.59e-140

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: 405.52  E-value: 1.59e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  19 MLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATGGRGSGGLAGGSGAaNSAFCLASTSPTS 98
Cdd:cd22549    1 MLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATSRASGGLASGTGTA-NSAFCLASTSPTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  99 SAFSSDYGGLFSNSAAAAAaaagvsPQEAGGQSAFISKVHTTAaDGLYPRVGMAHPYESWYKSGFHSTLAAgeVTNGAAS 178
Cdd:cd22549   80 SAFSSDYSGLFSNSTSVAT------PSQESGQSAFISKVHTSA-ESLYPRVGMAHPYESWYKSGFHSTISG--DVSGGAS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 179 SWWDVHSSPGSWLEVQNPAGGLQSSLHSGAPQASLHSQLGTYNPDFSSLTHSAFSSTGLGssaAAASHLLSTSQHLLAQD 258
Cdd:cd22549  151 SWWDVHTNPSSWLEVQNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFSSTGIS---ATASHLLSTSQHLLTQE 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223646113 259 GFKPVLPsysDSSAAVAAAAASAMISGAAAAAAGGSSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 333
Cdd:cd22549  228 GFKPVLP---SYTDSSAANAMGSASIISGAATLGGGSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
zf-H2C2_2 pfam13465
Zinc-finger double domain;
378-401 2.47e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 2.47e-06
                          10        20
                  ....*....|....*....|....
gi 223646113  378 ELQRHLRTHTGEKRFACPVCNKRF 401
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-375 1.70e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.70e-04
                          10        20
                  ....*....|....*....|....*...
gi 223646113  348 HLKAHLRWHTGERPFVCNwlFCGKRFTR 375
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 ...
 392-414 2.80e-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: 38.05  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|...
gi 223646113  392 FACPVCNKRFMRSDHLSKHIKTH 414
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 19-333 1.59e-140

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: 405.52  E-value: 1.59e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  19 MLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATGGRGSGGLAGGSGAaNSAFCLASTSPTS 98
Cdd:cd22549    1 MLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATSRASGGLASGTGTA-NSAFCLASTSPTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  99 SAFSSDYGGLFSNSAAAAAaaagvsPQEAGGQSAFISKVHTTAaDGLYPRVGMAHPYESWYKSGFHSTLAAgeVTNGAAS 178
Cdd:cd22549   80 SAFSSDYSGLFSNSTSVAT------PSQESGQSAFISKVHTSA-ESLYPRVGMAHPYESWYKSGFHSTISG--DVSGGAS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 179 SWWDVHSSPGSWLEVQNPAGGLQSSLHSGAPQASLHSQLGTYNPDFSSLTHSAFSSTGLGssaAAASHLLSTSQHLLAQD 258
Cdd:cd22549  151 SWWDVHTNPSSWLEVQNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFSSTGIS---ATASHLLSTSQHLLTQE 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223646113 259 GFKPVLPsysDSSAAVAAAAASAMISGAAAAAAGGSSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 333
Cdd:cd22549  228 GFKPVLP---SYTDSSAANAMGSASIISGAATLGGGSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
zf-H2C2_2 pfam13465
Zinc-finger double domain;
378-401 2.47e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 2.47e-06
                          10        20
                  ....*....|....*....|....
gi 223646113  378 ELQRHLRTHTGEKRFACPVCNKRF 401
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-375 1.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.70e-04
                          10        20
                  ....*....|....*....|....*...
gi 223646113  348 HLKAHLRWHTGERPFVCNwlFCGKRFTR 375
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 ...
 392-414 2.80e-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: 38.05  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|...
gi 223646113  392 FACPVCNKRFMRSDHLSKHIKTH 414
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 361-415 8.10e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 8.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223646113 361 PFVCNwlFCGKRFTRSDELQRHLRTHTGEKrfACPVCNKRFMRSDHLSKHI-KTHN 415
Cdd:PHA00733  73 PYVCP--LCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKHN 124
ZnF_C2H2 smart00355
zinc finger;
392-414 6.23e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.36  E-value: 6.23e-03
                           10        20
                   ....*....|....*....|...
gi 223646113   392 FACPVCNKRFMRSDHLSKHIKTH 414
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
347-415 8.62e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 8.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223646113 347 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACP--VCNKRFMRSDHLSKHIKTHN 415
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQ 377
 
Name Accession Description Interval E-value
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 19-333 1.59e-140

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: 405.52  E-value: 1.59e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  19 MLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATGGRGSGGLAGGSGAaNSAFCLASTSPTS 98
Cdd:cd22549    1 MLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATSRASGGLASGTGTA-NSAFCLASTSPTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  99 SAFSSDYGGLFSNSAAAAAaaagvsPQEAGGQSAFISKVHTTAaDGLYPRVGMAHPYESWYKSGFHSTLAAgeVTNGAAS 178
Cdd:cd22549   80 SAFSSDYSGLFSNSTSVAT------PSQESGQSAFISKVHTSA-ESLYPRVGMAHPYESWYKSGFHSTISG--DVSGGAS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 179 SWWDVHSSPGSWLEVQNPAGGLQSSLHSGAPQASLHSQLGTYNPDFSSLTHSAFSSTGLGssaAAASHLLSTSQHLLAQD 258
Cdd:cd22549  151 SWWDVHTNPSSWLEVQNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFSSTGIS---ATASHLLSTSQHLLTQE 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223646113 259 GFKPVLPsysDSSAAVAAAAASAMISGAAAAAAGGSSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 333
Cdd:cd22549  228 GFKPVLP---SYTDSSAANAMGSASIISGAATLGGGSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 19-333 4.24e-76

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: 241.02  E-value: 4.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  19 MLAATCNKIGNTSPL-TTLPESSAFAKGGFHPWKRSSSSCNLGSSL-SGFAVATGGRGSGGL----AGGSGAANSAFCLA 92
Cdd:cd22538    1 MLAATCNKIGSPSPSpSSLSDSSSSFGKGFHPWKRSSSSSSSLGSSlSGFGVSGSSRNGNLVsdsfSCNGSPGSSAFSLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  93 STSPTSSAFSSDYGgLFSNSAaaaaaaaGVSPQEAGGQSAFISKVHTT--AADGLYPRVGMAHPYESWYKSGfHSTLAAG 170
Cdd:cd22538   81 SSTSSTSPFANEYS-VFQAPV-------SSGSQEASHQPVFISKVHTSvdSLQGIYPRVGMAHPYESWFKPS-HPGIATG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 171 EVTNGAaSSWWDVHSSpgsWLEVQNPAGG-LQSSLHSGAPQASLHSQLGTYNPDFSSLTHSAFSStglgssaAAASHLLS 249
Cdd:cd22538  152 EGGGGA-SSWWDVGAG---WIDVQNPNGAaLQTSLHSGGLQTSLHSPLGGYNSDYSGLGHSAFST-------GASSHLLT 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 250 TSQHLLaqDGFKPVLPSYSDSSAAVAAAAASAMISGAAAAAA-GGSSARSARRYSGRATCDCPNCQEAERLGPAGASLRR 328
Cdd:cd22538  221 TGQHLM--DGFKPVLPPSYPDSSPSPLAGAGGSMLTGGPTAPlGGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRR 298


                 ....*
gi 223646113 329 KGLHS 333
Cdd:cd22538  299 KGLHS 303
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 2-333 2.27e-52

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: 178.94  E-value: 2.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113   2 ATSILGEEPRFGTTPLAMLAATCNKIGNTSPLTtlpESSAFAKGGFHPWKRSSSSCNLGSSLSGFAvatGGRGSGGLAGG 81
Cdd:cd22542    1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIR---DSATPGKPGNNPGKKPYSLGSDLSSAKSRS---SELMGDSYTAT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  82 SGAANSAFCLASTSPTSSAFSSDYGGlFSNSAaaaaaaagvsPQEAGGQ--SAFISKVHTTA--ADGLYPRVGMAHPYES 157
Cdd:cd22542   75 FSSGNGLMSPSGSPQASTTYGNDYNP-FSHSF----------PTSSGSQdpSLLVSKGHPSAdcLPSVYTSLDMAHPYGS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 158 WYKSGFHSTLAAGevTNGAASSWWDVHSSpGSWLEVQNPAGGLQSSLHSGAPQASLHSQLGTYNPDFSsLTHSAFSSTGL 237
Cdd:cd22542  144 WYKTGIHPGISSS--STNATASWWDMHSN-TNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYTEFTT-LNPAPYPAVGI 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 238 GSSaaaaSHLLSTSQHLLAQDGFKPVLPSYSDSSAAVAAAAASAMISGAAAaaaggssarsarrySGRATCDCPNCQEAE 317
Cdd:cd22542  220 SSS----SHLLPSSQHMLSQDMYKPKPVANNGLMEGGIGLKSPSGGSYGST--------------TGRSSCDCPNCQELE 281

                        330
                 ....*....|....*.
gi 223646113 318 RLGPAGASLRRKGLHS 333
Cdd:cd22542  282 RLGASAASLRKKPIHS 297
SP6-9-like_N cd22547
N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to ...
 19-333 1.04e-41

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: 147.94  E-value: 1.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  19 MLAATCNKIGNTSPlTTLPESsAFAKGgFHPWKRsssscnlgsslsgfavatggrgsgglaggsgaansafclasTSPTS 98
Cdd:cd22547    1 MLAAQCNKLSSKSP-PPLADA-AVGKG-FHPWKK-----------------------------------------SPPSV 36

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  99 SAFSSdygglfsnsaaaaaaaagvspqeaggQSAFISKVHTTAADgLYPRVGmAHPYESWYKSGFHSTLAAGEVTNGA-- 176
Cdd:cd22547   37 SSNSS--------------------------QASLLQKVHSSVSD-SRPVYS-HHPYESWPFNATSHHHKKEEVSSSAnn 88

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 177 ASSWWDVHSSPGSWL-EVQNPAGGLQSSLHSGAPqaslhsqlgtyNPDFSSLTHSAFSStglgssaaaaSHLLSTSQHLL 255
Cdd:cd22547   89 SSSWWDMHSAAGSWLdESSAAATGPHSQISPNYP-----------SSDYSLGHLLASSS----------APLLLSGQHLL 147

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223646113 256 aQDGFKPVLPSYSDSSAAVAAAAASAMISGAAAAAAGGSsarsaRRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 333
Cdd:cd22547  148 -QDTYKSMLPSQGDIGASSFPSSLLSQPSLSGVPSPRSQ-----RRYTGRATCDCPNCQEAERLGPAGAHLRKKNIHS 219
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 19-333 1.77e-39

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: 140.46  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  19 MLAATCNKIGNTSPLTTLPesSAFAKGGFHPWKRsssscnlgsslsgfavatggrgsgglaggsgaansafclastspts 98
Cdd:cd22543    1 MLAATCNKLGSQSPLPPSD--SAFGKGGFHPWKR---------------------------------------------- 32

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113  99 safssdygglfsnsaaaaaaaagvspqeaggqsafiskvhttaadglYPRVGMAHPYESWYKSGFHSTLAAGEVTNGAAS 178
Cdd:cd22543   33 -----------------------------------------------SSSLDMAHPYESWFKPGHHATIAPGEVPSNEAS 65

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 179 SWWDVHSsPGSWLEVqnpagglqsslhsgapqaslhsqlgtynpdfsslthsafsstglgssaaaaSHLLST-SQHLLAQ 257
Cdd:cd22543   66 SWWDVHP-GGSWLDV---------------------------------------------------PHLLSPgGQHLLGQ 93

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223646113 258 DGFKPVLPSYSDSSAAVAAAAASAMISGAAAAAAGgssarsaRRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 333
Cdd:cd22543   94 DGYKPVLPGASPESAGSDGSSLPGAASGGGSRRSA-------RRYSGRATCDCPNCQEAERLGPAGAGLRKKGLHS 162
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 145-332 8.28e-24

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: 99.99  E-value: 8.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 145 LYPRVGMAHPYESWyksgFHSTLAAGEVTNGAASSWWDVHSSpGSWLEVQNPAGGLQSSLHSGAPQASLhsqlGTYNPDf 224
Cdd:cd22544   94 LHPPPDMAHPYESW----FRPPHPGGSGEEGGVPSWWDLHAG-SSWMDLQHGQGGLQSPGPPGGLQPPL----GGYGSE- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223646113 225 SSLthsafsstglgssAAAASHLLSTSQHLLAQDGFKPVLPSYSDSSAAVAAAAASAMISGAaaaaaggssarsarRYSG 304
Cdd:cd22544  164 HQL-------------CGPPHHLLPPAQHLMGQEGPKLLEHPAEDPSLDGSPRPKGSRRSVP--------------RSSG 216

                        170       180
                 ....*....|....*....|....*...
gi 223646113 305 RATCDCPNCQEAERLGPAGASLRRKGLH 332
Cdd:cd22544  217 QAACRCPNCQEAERLGPPPDGGKKKHLH 244
zf-H2C2_2 pfam13465
Zinc-finger double domain;
378-401 2.47e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 2.47e-06
                          10        20
                  ....*....|....*....|....
gi 223646113  378 ELQRHLRTHTGEKRFACPVCNKRF 401
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-375 1.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.70e-04
                          10        20
                  ....*....|....*....|....*...
gi 223646113  348 HLKAHLRWHTGERPFVCNwlFCGKRFTR 375
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 ...
 392-414 2.80e-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: 38.05  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|...
gi 223646113  392 FACPVCNKRFMRSDHLSKHIKTH 414
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 362-386 7.11e-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: 36.89  E-value: 7.11e-04
                          10        20
                  ....*....|....*....|....*
gi 223646113  362 FVCNwlFCGKRFTRSDELQRHLRTH 386
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 361-415 8.10e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 8.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223646113 361 PFVCNwlFCGKRFTRSDELQRHLRTHTGEKrfACPVCNKRFMRSDHLSKHI-KTHN 415
Cdd:PHA00733  73 PYVCP--LCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKHN 124
ZnF_C2H2 smart00355
zinc finger;
392-414 6.23e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.36  E-value: 6.23e-03
                           10        20
                   ....*....|....*....|...
gi 223646113   392 FACPVCNKRFMRSDHLSKHIKTH 414
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
347-415 8.62e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 8.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223646113 347 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACP--VCNKRFMRSDHLSKHIKTHN 415
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQ 377
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 15-40 9.01e-03

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; 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 chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 35.50  E-value: 9.01e-03
                         10        20
                 ....*....|....*....|....*.
gi 223646113  15 TPLAMLAATCNKIGNTSPLTTLPESS 40
Cdd:cd22545   10 SPLALLAATCSKIGSPAENSTGPGGN 35
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 392-414 9.37e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 33.77  E-value: 9.37e-03
                          10        20
                  ....*....|....*....|...
gi 223646113  392 FACPVCNKRFMRSDHLSKHIKTH 414
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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