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Conserved domains on  [gi|664806069|ref|NP_001287766|]
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transcription factor Sp7 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP6-9_N super family cl41771
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 1-277 1.59e-115

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.


The actual alignment was detected with superfamily member cd22542:

Pssm-ID: 425402 [Multi-domain]  Cd Length: 297  Bit Score: 339.18  E-value: 1.59e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   1 MLTAACSKFGGSSPLRDSTTLGKAG---TKKPYSVGSDLS-----ASKTMGDAYPAPFTSTNGLLSPAGSPPAPTsGYAN 72
Cdd:cd22542   18 MLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYSLGSDLSsaksrSSELMGDSYTATFSSGNGLMSPSGSPQAST-TYGN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  73 DYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPgGNWLGG 152
Cdd:cd22542   97 DYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTNATASWWDMHS-NTNWLS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 153 GQGQGDGLQGTLPTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDVYKPKAVGNSGQLEGSGG 227
Cdd:cd22542  176 AQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDMYKPKPVANNGLMEGGIG 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 664806069 228 AKPPrgastggSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 277
Cdd:cd22542  255 LKSP-------SGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-347 6.98e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 6.98e-06
                          10        20
                  ....*....|....*....|....*.
gi 664806069  322 ELERHVRTHTREKKFTCLLCSKRFTR 347
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-319 7.63e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 7.63e-05
                          10        20
                  ....*....|....*....|....*...
gi 664806069  292 HLKAHLRWHTGERPFVCNwlFCGKRFTR 319
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
 
Name Accession Description Interval E-value
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 1-277 1.59e-115

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: 339.18  E-value: 1.59e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   1 MLTAACSKFGGSSPLRDSTTLGKAG---TKKPYSVGSDLS-----ASKTMGDAYPAPFTSTNGLLSPAGSPPAPTsGYAN 72
Cdd:cd22542   18 MLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYSLGSDLSsaksrSSELMGDSYTATFSSGNGLMSPSGSPQAST-TYGN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  73 DYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPgGNWLGG 152
Cdd:cd22542   97 DYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTNATASWWDMHS-NTNWLS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 153 GQGQGDGLQGTLPTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDVYKPKAVGNSGQLEGSGG 227
Cdd:cd22542  176 AQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDMYKPKPVANNGLMEGGIG 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 664806069 228 AKPPrgastggSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 277
Cdd:cd22542  255 LKSP-------SGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-347 6.98e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 6.98e-06
                          10        20
                  ....*....|....*....|....*.
gi 664806069  322 ELERHVRTHTREKKFTCLLCSKRFTR 347
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-319 7.63e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 7.63e-05
                          10        20
                  ....*....|....*....|....*...
gi 664806069  292 HLKAHLRWHTGERPFVCNwlFCGKRFTR 319
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-231 2.14e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069    3 TAACSKFGGSSPLRDSTTLGKAGTKKPYSVGSDLSASKTMGDAYPAPFTSTNGLLSPAGSPP--APTSGYANDYPPFSHS 80
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPavASLSESRESLPSPWDP 2804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   81 FPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDM-----------THPYGSWYKAGIHAGISPGPGNTP-TPWWDMHPGGN 148
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTapppppgppppSLPLGGSVAPGGDVRRRPPSRSPAaKPAAPARPPVR 2884

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  149 WLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGpqhvLPQDVYKPKAvGNSGQLEGSGGA 228
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPTT-DPAGAGEPSGAV 2959


                  ...
gi 664806069  229 KPP 231
Cdd:PHA03247 2960 PQP 2962
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
291-358 6.64e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 6.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664806069 291 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLL--CSKRFTRSDHLSKHQRTH 358
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ 376
 
Name Accession Description Interval E-value
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 1-277 1.59e-115

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: 339.18  E-value: 1.59e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   1 MLTAACSKFGGSSPLRDSTTLGKAG---TKKPYSVGSDLS-----ASKTMGDAYPAPFTSTNGLLSPAGSPPAPTsGYAN 72
Cdd:cd22542   18 MLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYSLGSDLSsaksrSSELMGDSYTATFSSGNGLMSPSGSPQAST-TYGN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  73 DYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPgGNWLGG 152
Cdd:cd22542   97 DYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTNATASWWDMHS-NTNWLS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 153 GQGQGDGLQGTLPTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDVYKPKAVGNSGQLEGSGG 227
Cdd:cd22542  176 AQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDMYKPKPVANNGLMEGGIG 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 664806069 228 AKPPrgastggSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 277
Cdd:cd22542  255 LKSP-------SGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 1-277 1.13e-36

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: 135.50  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   1 MLTAACSKFGGSSPLR---DSTTLGKAGT---KKPYS---VGSDLSASKTMGDAYPAPFTSTNGLLSPA---GSPPAPTS 68
Cdd:cd22549    1 MLAATCNKIGNTSPLTtlpESSAFAKGGFhpwKRSSSscnLGSSLSGFAVATSRASGGLASGTGTANSAfclASTSPTSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  69 GYANDYPPFSHSFPGPTGTQDPG---LLVPKGHSSSDclpSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHP 145
Cdd:cd22549   81 AFSSDYSGLFSNSTSVATPSQESgqsAFISKVHTSAE---SLYPRVGMAHPYESWYKSGFHSTISGDVSGGASSWWDVHT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 146 GGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPY-------PAPHLLqPGPQHVLPQDVYKPKAVGN 218
Cdd:cd22549  158 NPSSWLEVQNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFsstgisaTASHLL-STSQHLLTQEGFKPVLPSY 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806069 219 SGQLEGSGGAKPPRGASTGGSGGYGGSG----AGRSSCDCPNCQELERLGAAAAGLRKKPIHS 277
Cdd:cd22549  237 TDSSAANAMGSASIISGAATLGGGSARSarrySGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 106-277 2.83e-36

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: 130.45  E-value: 2.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 106 SVYTSLDMTHPYGSWYKAGIHAGISPG--PGNTPTPWWDMHPGGNWLGGgqgqgdglqgtlptgpaqpplnpqlptypsd 183
Cdd:cd22543   31 KRSSSLDMAHPYESWFKPGHHATIAPGevPSNEASSWWDVHPGGSWLDV------------------------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 184 faplnpapypaPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGGAKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERL 263
Cdd:cd22543   80 -----------PHLLSPGGQHLLGQDGYKPVLPGASPESAGSDGSSLPGAASGGGSRRSARRYSGRATCDCPNCQEAERL 148

                        170
                 ....*....|....
gi 664806069 264 GAAAAGLRKKPIHS 277
Cdd:cd22543  149 GPAGAGLRKKGLHS 162
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 1-277 1.32e-21

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: 94.26  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   1 MLTAACSKFGGSSP----LRD-STTLGKA------GTKKPYSVGSDLSA-----SKTMGDAYPAPFTSTNGLLSPA---G 61
Cdd:cd22538    1 MLAATCNKIGSPSPspssLSDsSSSFGKGfhpwkrSSSSSSSLGSSLSGfgvsgSSRNGNLVSDSFSCNGSPGSSAfslT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  62 SPPAPTSGYANDYPPFSHsfPGPTGTQDPG---LLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGiHAGISPGPGNT-P 137
Cdd:cd22538   81 SSTSSTSPFANEYSVFQA--PVSSGSQEAShqpVFISKVHTSVDSLQGIYPRVGMAHPYESWFKPS-HPGIATGEGGGgA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 138 TPWWDMHPGGNWLGGGQGQGDGLqgTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYP---APHLLQPGpQHVLpqDVYKPK 214
Cdd:cd22538  158 SSWWDVGAGWIDVQNPNGAALQT--SLHSGGLQTSLHSPLGGYNSDYSGLGHSAFStgaSSHLLTTG-QHLM--DGFKPV 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664806069 215 AVGN-----SGQLEGSGG---AKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 277
Cdd:cd22538  233 LPPSypdssPSPLAGAGGsmlTGGPTAPLGGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
SP6-9-like_N cd22547
N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to ...
 62-277 9.47e-19

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: 84.39  E-value: 9.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  62 SPPAPTSGYANDYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSldmtHPYGSWYKAGIHAGISPGPG----NTP 137
Cdd:cd22547   14 PPPLADAAVGKGFHPWKKSPPSVSSNSSQASLLQKVHSSVSDSRPVYSH----HPYESWPFNATSHHHKKEEVsssaNNS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 138 TPWWDMHPGGNWLGggqgqgdglqgTLPTGPAQPPLNPQLPTYP-SDFAPLNPAPYPAPHLLQPGPQhvLPQDVYK---P 213
Cdd:cd22547   90 SSWWDMHSAAGSWL-----------DESSAAATGPHSQISPNYPsSDYSLGHLLASSSAPLLLSGQH--LLQDTYKsmlP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664806069 214 KAvGNSGQLEGSGGAKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 277
Cdd:cd22547  157 SQ-GDIGASSFPSSLLSQPSLSGVPSPRSQRRYTGRATCDCPNCQEAERLGPAGAHLRKKNIHS 219
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 1-276 3.01e-12

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: 66.10  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   1 MLTAACSKFGG--SSPLRDSTTLGKAGTKKPYSVGSDlsasktmGDAYPAPFTSTNGLLSPAGSPPAPTSGYANDYPPFS 78
Cdd:cd22544    1 MLTAVCGSLGNqhSETPRASPPTLDLQPLQPYQIHSS-------PEAGDYPSPLQPTELQSLPLGPGVDFSARESYEPHS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  79 hsfpGPTGTQDPGLLVPKGHSSSDCLPSvytsLDMTHPYGSWYKAGiHAGISPGPGNTPtPWWDMHPGGNWLGGGQGQGD 158
Cdd:cd22544   74 ----SRRTCLDLESDLPLGPFPKLLHPP----PDMAHPYESWFRPP-HPGGSGEEGGVP-SWWDLHAGSSWMDLQHGQGG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069 159 GLQgTLPTGPAQPPLNpqlpTYPSDfaplNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGGAKPprgastgg 238
Cdd:cd22544  144 LQS-PGPPGGLQPPLG----GYGSE----HQLCGPPHHLLPPAQHLMGQEGPKLLEHPAEDPSLDGSPRPKG-------- 206

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 664806069 239 SGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIH 276
Cdd:cd22544  207 SRRSVPRSSGQAACRCPNCQEAERLGPPPDGGKKKHLH 244
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-347 6.98e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 6.98e-06
                          10        20
                  ....*....|....*....|....*.
gi 664806069  322 ELERHVRTHTREKKFTCLLCSKRFTR 347
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 336-358 5.80e-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: 39.59  E-value: 5.80e-05
                          10        20
                  ....*....|....*....|...
gi 664806069  336 FTCLLCSKRFTRSDHLSKHQRTH 358
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-319 7.63e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 7.63e-05
                          10        20
                  ....*....|....*....|....*...
gi 664806069  292 HLKAHLRWHTGERPFVCNwlFCGKRFTR 319
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-231 2.14e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069    3 TAACSKFGGSSPLRDSTTLGKAGTKKPYSVGSDLSASKTMGDAYPAPFTSTNGLLSPAGSPP--APTSGYANDYPPFSHS 80
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPavASLSESRESLPSPWDP 2804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069   81 FPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDM-----------THPYGSWYKAGIHAGISPGPGNTP-TPWWDMHPGGN 148
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTapppppgppppSLPLGGSVAPGGDVRRRPPSRSPAaKPAAPARPPVR 2884

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806069  149 WLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGpqhvLPQDVYKPKAvGNSGQLEGSGGA 228
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPTT-DPAGAGEPSGAV 2959


                  ...
gi 664806069  229 KPP 231
Cdd:PHA03247 2960 PQP 2962
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 306-330 4.91e-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: 37.28  E-value: 4.91e-04
                          10        20
                  ....*....|....*....|....*
gi 664806069  306 FVCNwlFCGKRFTRSDELERHVRTH 330
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
291-358 6.64e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 6.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664806069 291 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLL--CSKRFTRSDHLSKHQRTH 358
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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