NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|291045138|ref|NP_001166938|]
View 

transcription factor Sp7 isoform a [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SP7_N cd22542
N-terminal domain of transcription factor Specificity Protein (SP) 7; Specificity Proteins ...
 2-295 2.66e-126

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: 367.30  E-value: 2.66e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   2 ASSLLEEEVHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKAG---TKKPYSVGSDLS-----ASKTMGDAYPAPFTSTNG 73
Cdd:cd22542    1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYSLGSDLSsaksrSSELMGDSYTATFSSGNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  74 LLSPAGSPPAPTsGYANDYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGN 153
Cdd:cd22542   81 LMSPSGSPQAST-TYGNDYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 154 TPTPWWDMHPgGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDV 228
Cdd:cd22542  160 ATASWWDMHS-NTNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDM 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291045138 229 YKPKAVGNSGQLEGSGGAKPPrgastggSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 295
Cdd:cd22542  238 YKPKPVANNGLMEGGIGLKSP-------SGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-365 6.53e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 6.53e-06
                          10        20
                  ....*....|....*....|....*.
gi 291045138  340 ELERHVRTHTREKKFTCLLCSKRFTR 365
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-337 7.28e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.28e-05
                          10        20
                  ....*....|....*....|....*...
gi 291045138  310 HLKAHLRWHTGERPFVCNwlFCGKRFTR 337
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 ...
 2-295 2.66e-126

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: 367.30  E-value: 2.66e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   2 ASSLLEEEVHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKAG---TKKPYSVGSDLS-----ASKTMGDAYPAPFTSTNG 73
Cdd:cd22542    1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYSLGSDLSsaksrSSELMGDSYTATFSSGNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  74 LLSPAGSPPAPTsGYANDYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGN 153
Cdd:cd22542   81 LMSPSGSPQAST-TYGNDYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 154 TPTPWWDMHPgGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDV 228
Cdd:cd22542  160 ATASWWDMHS-NTNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDM 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291045138 229 YKPKAVGNSGQLEGSGGAKPPrgastggSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 295
Cdd:cd22542  238 YKPKPVANNGLMEGGIGLKSP-------SGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-365 6.53e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 6.53e-06
                          10        20
                  ....*....|....*....|....*.
gi 291045138  340 ELERHVRTHTREKKFTCLLCSKRFTR 365
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 14-249 3.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   14 SSPLAMLTAACSKFGGSSPLRDSTTLGKAGTKKPYSVGSDLSASKTMGDAYPAPFTSTNGLLSPAGSPP--APTSGYAND 91
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPavASLSESRES 2797

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   92 YPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDM-----------THPYGSWYKAGIHAGISPGPGNTP-TPWW 159
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTapppppgppppSLPLGGSVAPGGDVRRRPPSRSPAaKPAA 2877

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  160 DMHPGGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGpqhvLPQDVYKPKAvGNSGQ 239
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPTT-DPAGA 2952

                         250
                  ....*....|
gi 291045138  240 LEGSGGAKPP 249
Cdd:PHA03247 2953 GEPSGAVPQP 2962
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-337 7.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.28e-05
                          10        20
                  ....*....|....*....|....*...
gi 291045138  310 HLKAHLRWHTGERPFVCNwlFCGKRFTR 337
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-376 7.58e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 7.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291045138 309 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLL--CSKRFTRSDHLSKHQRTH 376
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 ...
 2-295 2.66e-126

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: 367.30  E-value: 2.66e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   2 ASSLLEEEVHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKAG---TKKPYSVGSDLS-----ASKTMGDAYPAPFTSTNG 73
Cdd:cd22542    1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYSLGSDLSsaksrSSELMGDSYTATFSSGNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  74 LLSPAGSPPAPTsGYANDYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGN 153
Cdd:cd22542   81 LMSPSGSPQAST-TYGNDYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 154 TPTPWWDMHPgGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDV 228
Cdd:cd22542  160 ATASWWDMHS-NTNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDM 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291045138 229 YKPKAVGNSGQLEGSGGAKPPrgastggSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 295
Cdd:cd22542  238 YKPKPVANNGLMEGGIGLKSP-------SGGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 19-295 2.69e-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: 135.11  E-value: 2.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  19 MLTAACSKFGGSSPLR---DSTTLGKAGT---KKPYS---VGSDLSASKTMGDAYPAPFTSTNGLLSPA---GSPPAPTS 86
Cdd:cd22549    1 MLAATCNKIGNTSPLTtlpESSAFAKGGFhpwKRSSSscnLGSSLSGFAVATSRASGGLASGTGTANSAfclASTSPTSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  87 GYANDYPPFSHSFPGPTGTQDPG---LLVPKGHSSSDclpSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHP 163
Cdd:cd22549   81 AFSSDYSGLFSNSTSVATPSQESgqsAFISKVHTSAE---SLYPRVGMAHPYESWYKSGFHSTISGDVSGGASSWWDVHT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 164 GGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPY-------PAPHLLqPGPQHVLPQDVYKPKAVGN 236
Cdd:cd22549  158 NPSSWLEVQNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFsstgisaTASHLL-STSQHLLTQEGFKPVLPSY 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045138 237 SGQLEGSGGAKPPRGASTGGSGGYGGSG----AGRSSCDCPNCQELERLGAAAAGLRKKPIHS 295
Cdd:cd22549  237 TDSSAANAMGSASIISGAATLGGGSARSarrySGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 124-295 3.31e-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: 3.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 124 SVYTSLDMTHPYGSWYKAGIHAGISPG--PGNTPTPWWDMHPGGNWLGGgqgqgdglqgtlptgpaqpplnpqlptypsd 201
Cdd:cd22543   31 KRSSSLDMAHPYESWFKPGHHATIAPGevPSNEASSWWDVHPGGSWLDV------------------------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 202 faplnpapypaPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGGAKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERL 281
Cdd:cd22543   80 -----------PHLLSPGGQHLLGQDGYKPVLPGASPESAGSDGSSLPGAASGGGSRRSARRYSGRATCDCPNCQEAERL 148

                        170
                 ....*....|....
gi 291045138 282 GAAAAGLRKKPIHS 295
Cdd:cd22543  149 GPAGAGLRKKGLHS 162
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
 19-295 1.66e-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: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  19 MLTAACSKFGGSSP----LRD-STTLGKA------GTKKPYSVGSDLSA-----SKTMGDAYPAPFTSTNGLLSPA---G 79
Cdd:cd22538    1 MLAATCNKIGSPSPspssLSDsSSSFGKGfhpwkrSSSSSSSLGSSLSGfgvsgSSRNGNLVSDSFSCNGSPGSSAfslT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  80 SPPAPTSGYANDYPPFSHsfPGPTGTQDPG---LLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGiHAGISPGPGNT-P 155
Cdd:cd22538   81 SSTSSTSPFANEYSVFQA--PVSSGSQEAShqpVFISKVHTSVDSLQGIYPRVGMAHPYESWFKPS-HPGIATGEGGGgA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 156 TPWWDMHPGGNWLGGGQGQGDGLqgTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYP---APHLLQPGpQHVLpqDVYKPK 232
Cdd:cd22538  158 SSWWDVGAGWIDVQNPNGAALQT--SLHSGGLQTSLHSPLGGYNSDYSGLGHSAFStgaSSHLLTTG-QHLM--DGFKPV 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291045138 233 AVGN-----SGQLEGSGG---AKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 295
Cdd:cd22538  233 LPPSypdssPSPLAGAGGsmlTGGPTAPLGGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
SP6-9-like_N cd22547
N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to ...
 80-295 1.16e-18

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: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  80 SPPAPTSGYANDYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSldmtHPYGSWYKAGIHAGISPGPG----NTP 155
Cdd:cd22547   14 PPPLADAAVGKGFHPWKKSPPSVSSNSSQASLLQKVHSSVSDSRPVYSH----HPYESWPFNATSHHHKKEEVsssaNNS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 156 TPWWDMHPGGNWLGggqgqgdglqgTLPTGPAQPPLNPQLPTYP-SDFAPLNPAPYPAPHLLQPGPQhvLPQDVYK---P 231
Cdd:cd22547   90 SSWWDMHSAAGSWL-----------DESSAAATGPHSQISPNYPsSDYSLGHLLASSSAPLLLSGQH--LLQDTYKsmlP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291045138 232 KAvGNSGQLEGSGGAKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHS 295
Cdd:cd22547  157 SQ-GDIGASSFPSSLLSQPSLSGVPSPRSQRRYTGRATCDCPNCQEAERLGPAGAHLRKKNIHS 219
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 19-294 2.31e-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: 66.48  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  19 MLTAACSKFGG--SSPLRDSTTLGKAGTKKPYSVGSDlsasktmGDAYPAPFTSTNGLLSPAGSPPAPTSGYANDYPPFS 96
Cdd:cd22544    1 MLTAVCGSLGNqhSETPRASPPTLDLQPLQPYQIHSS-------PEAGDYPSPLQPTELQSLPLGPGVDFSARESYEPHS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  97 hsfpGPTGTQDPGLLVPKGHSSSDCLPSvytsLDMTHPYGSWYKAGiHAGISPGPGNTPtPWWDMHPGGNWLGGGQGQGD 176
Cdd:cd22544   74 ----SRRTCLDLESDLPLGPFPKLLHPP----PDMAHPYESWFRPP-HPGGSGEEGGVP-SWWDLHAGSSWMDLQHGQGG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138 177 GLQgTLPTGPAQPPLNpqlpTYPSDfaplNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGGAKPprgastgg 256
Cdd:cd22544  144 LQS-PGPPGGLQPPLG----GYGSE----HQLCGPPHHLLPPAQHLMGQEGPKLLEHPAEDPSLDGSPRPKG-------- 206

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 291045138 257 SGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIH 294
Cdd:cd22544  207 SRRSVPRSSGQAACRCPNCQEAERLGPPPDGGKKKHLH 244
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-365 6.53e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 6.53e-06
                          10        20
                  ....*....|....*....|....*.
gi 291045138  340 ELERHVRTHTREKKFTCLLCSKRFTR 365
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 14-249 3.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   14 SSPLAMLTAACSKFGGSSPLRDSTTLGKAGTKKPYSVGSDLSASKTMGDAYPAPFTSTNGLLSPAGSPP--APTSGYAND 91
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPavASLSESRES 2797

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138   92 YPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDM-----------THPYGSWYKAGIHAGISPGPGNTP-TPWW 159
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTapppppgppppSLPLGGSVAPGGDVRRRPPSRSPAaKPAA 2877

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045138  160 DMHPGGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGpqhvLPQDVYKPKAvGNSGQ 239
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPTT-DPAGA 2952

                         250
                  ....*....|
gi 291045138  240 LEGSGGAKPP 249
Cdd:PHA03247 2953 GEPSGAVPQP 2962
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 354-376 5.27e-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: 39.98  E-value: 5.27e-05
                          10        20
                  ....*....|....*....|...
gi 291045138  354 FTCLLCSKRFTRSDHLSKHQRTH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-337 7.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.28e-05
                          10        20
                  ....*....|....*....|....*...
gi 291045138  310 HLKAHLRWHTGERPFVCNwlFCGKRFTR 337
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 ...
 324-348 4.51e-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: 4.51e-04
                          10        20
                  ....*....|....*....|....*
gi 291045138  324 FVCNwlFCGKRFTRSDELERHVRTH 348
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-376 7.58e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 7.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291045138 309 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLL--CSKRFTRSDHLSKHQRTH 376
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH