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Conserved domains on  [gi|30913319|sp|Q8VI67|]
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RecName: Full=Transcription factor Sp7; AltName: Full=C22; AltName: Full=Zinc finger protein osterix

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; ...
2-292 1.14e-123

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: 360.37  E-value: 1.14e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319   2 ASSLLEEEAHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKGG---TKKPY---ADLSAPK-----TMGDAYPAPFSSTNG 70
Cdd:cd22542   1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYslgSDLSSAKsrsseLMGDSYTATFSSGNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  71 LLSPAGSPPAPaSGYANDYPPFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGN 150
Cdd:cd22542  81 LMSPSGSPQAS-TTYGNDYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 151 TPTPWWDMHPgGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDV 225
Cdd:cd22542 160 ATASWWDMHS-NTNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDM 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30913319 226 YKPKAVGNSGQLEGSGAAKPPRgagtggsGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHS 292
Cdd:cd22542 238 YKPKPVANNGLMEGGIGLKSPS-------GGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
337-362 8.29e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 8.29e-06
                          10        20
                  ....*....|....*....|....*.
gi 30913319   337 ELERHVRTHTREKKFTCLLCSKRFTR 362
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
307-334 9.24e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.24e-05
                          10        20
                  ....*....|....*....|....*...
gi 30913319   307 HLKAHLRWHTGERPFVCNwlFCGKRFTR 334
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 ...
2-292 1.14e-123

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: 360.37  E-value: 1.14e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319   2 ASSLLEEEAHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKGG---TKKPY---ADLSAPK-----TMGDAYPAPFSSTNG 70
Cdd:cd22542   1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYslgSDLSSAKsrsseLMGDSYTATFSSGNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  71 LLSPAGSPPAPaSGYANDYPPFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGN 150
Cdd:cd22542  81 LMSPSGSPQAS-TTYGNDYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 151 TPTPWWDMHPgGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDV 225
Cdd:cd22542 160 ATASWWDMHS-NTNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDM 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30913319 226 YKPKAVGNSGQLEGSGAAKPPRgagtggsGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHS 292
Cdd:cd22542 238 YKPKPVANNGLMEGGIGLKSPS-------GGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
zf-H2C2_2 pfam13465
Zinc-finger double domain;
337-362 8.29e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 8.29e-06
                          10        20
                  ....*....|....*....|....*.
gi 30913319   337 ELERHVRTHTREKKFTCLLCSKRFTR 362
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
16-247 6.75e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319    16 PLAMLTAACSKFGGSSPLRDSTTLGKGGTKKPYADLSAPKTMgdAYPAPFSSTNGLLSPAGSPPAPASGYAndypPFPHS 95
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSPWDPADPPA----AVLAP 2814
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319    96 FPGPTGAQDPGLLVPKGHSSSDCLPSVYTS-LDMTHPYGSWYKAGIHAGISPGPGNTP-TPWWDMHPGGNWLGGGQGQGD 173
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVAPGGDVRRRPPSRSPAaKPAAPARPPVRRLARPAVSRS 2894
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30913319   174 GLQGTLSTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGpqhvLPQDVYKPKAvGNSGQLEGSGAAKPPR 247
Cdd:PHA03247 2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPTT-DPAGAGEPSGAVPQPW 2963
zf-H2C2_2 pfam13465
Zinc-finger double domain;
307-334 9.24e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.24e-05
                          10        20
                  ....*....|....*....|....*...
gi 30913319   307 HLKAHLRWHTGERPFVCNwlFCGKRFTR 334
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP--ECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-373 8.04e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 8.04e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30913319 306 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLL--CSKRFTRSDHLSKHQRTH 373
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 ...
2-292 1.14e-123

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: 360.37  E-value: 1.14e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319   2 ASSLLEEEAHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKGG---TKKPY---ADLSAPK-----TMGDAYPAPFSSTNG 70
Cdd:cd22542   1 AASMLEEEARYGSSPLAMLTAACNKFGGSSPIRDSATPGKPGnnpGKKPYslgSDLSSAKsrsseLMGDSYTATFSSGNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  71 LLSPAGSPPAPaSGYANDYPPFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGN 150
Cdd:cd22542  81 LMSPSGSPQAS-TTYGNDYNPFSHSFPTSSGSQDPSLLVSKGHPSADCLPSVYTSLDMAHPYGSWYKTGIHPGISSSSTN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 151 TPTPWWDMHPgGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTY----PSDFAPLNPA-PYPAPHLLqPGPQHVLPQDV 225
Cdd:cd22542 160 ATASWWDMHS-NTNWLSAQGQPDGLQASLQPVPAQTPLNPQLPSYteftTLNPAPYPAVgISSSSHLL-PSSQHMLSQDM 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30913319 226 YKPKAVGNSGQLEGSGAAKPPRgagtggsGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHS 292
Cdd:cd22542 238 YKPKPVANNGLMEGGIGLKSPS-------GGSYGSTTGRSSCDCPNCQELERLGASAASLRKKPIHS 297
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
121-292 3.67e-38

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: 135.84  E-value: 3.67e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 121 SVYTSLDMTHPYGSWYKAGIHAGISPG--PGNTPTPWWDMHPGGNWLGGgqgqgdglqgtlstgpaqpplnpqlptypsd 198
Cdd:cd22543  31 KRSSSLDMAHPYESWFKPGHHATIAPGevPSNEASSWWDVHPGGSWLDV------------------------------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 199 faplnpapypaPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGAAKPPRGAGTGGSGGYAGSGAGRSTCDCPNCQELERL 278
Cdd:cd22543  80 -----------PHLLSPGGQHLLGQDGYKPVLPGASPESAGSDGSSLPGAASGGGSRRSARRYSGRATCDCPNCQEAERL 148
                       170
                ....*....|....
gi 30913319 279 GAAAAGLRKKPIHS 292
Cdd:cd22543 149 GPAGAGLRKKGLHS 162
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
19-292 8.91e-38

N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP9 plays a role in limb outgrowth. It is expressed during embryogenesis in the forming apical ectodermal ridge, restricted regions of the central nervous system, and tail bud. SP8 and SP9 are two closely related transcription factors that mediate FGF10 signaling, which in turn regulates FGF8 expression which is essential for normal limb development. Both SP8 and SP9 have been found in vertebrates, but only SP8 is present in invertebrates. SP9 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP9.


Pssm-ID: 411695 [Multi-domain]  Cd Length: 299  Bit Score: 138.97  E-value: 8.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  19 MLTAACSKFGGSSPLR---DSTTLGKGGT---KKPYAD------LSAPKTMGD----AYPAPFSSTNGLLSPAGSPPApA 82
Cdd:cd22549   1 MLAATCNKIGNTSPLTtlpESSAFAKGGFhpwKRSSSScnlgssLSGFAVATSrasgGLASGTGTANSAFCLASTSPT-S 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  83 SGYANDYPPFPHSFPGPTGAQDPG---LLVPKGHSSSDclpSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMH 159
Cdd:cd22549  80 SAFSSDYSGLFSNSTSVATPSQESgqsAFISKVHTSAE---SLYPRVGMAHPYESWYKSGFHSTISGDVSGGASSWWDVH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 160 PGGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTYPSDFAPLNPAPY-------PAPHLLqPGPQHVLPQDVYKPKAVG 232
Cdd:cd22549 157 TNPSSWLEVQNPAGGLQSSLHSGTPQASLHSQLGGYNPDFSSLTHSAFsstgisaTASHLL-STSQHLLTQEGFKPVLPS 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30913319 233 NSGQLEGSGAAKPPRGAGTGGSGGYAGSG----AGRSTCDCPNCQELERLGAAAAGLRKKPIHS 292
Cdd:cd22549 236 YTDSSAANAMGSASIISGAATLGGGSARSarrySGRATCDCPNCQEAERLGPAGASLRRKGLHS 299
SP8_N cd22538
N-terminal domain of transcription factor Specificity Protein (SP) 8; Specificity Proteins ...
19-292 9.58e-23

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: 97.73  E-value: 9.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  19 MLTAACSKFGGSSP----LRD-STTLGKG--GTKKPYADLSAPKTMGDAYPAPFSSTNGLL-----SPAGSPPAPA---- 82
Cdd:cd22538   1 MLAATCNKIGSPSPspssLSDsSSSFGKGfhPWKRSSSSSSSLGSSLSGFGVSGSSRNGNLvsdsfSCNGSPGSSAfslt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  83 ------SGYANDYPPFPHsfPGPTGAQDPG---LLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGiHAGISPGPGNT-P 152
Cdd:cd22538  81 sstsstSPFANEYSVFQA--PVSSGSQEAShqpVFISKVHTSVDSLQGIYPRVGMAHPYESWFKPS-HPGIATGEGGGgA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 153 TPWWDMHPGGNWLGGGQGQGDGLqgTLSTGPAQPPLNPQLPTYPSDFAPLNPAPYP---APHLLQPGpQHVLpqDVYKPK 229
Cdd:cd22538 158 SSWWDVGAGWIDVQNPNGAALQT--SLHSGGLQTSLHSPLGGYNSDYSGLGHSAFStgaSSHLLTTG-QHLM--DGFKPV 232
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30913319 230 AVGN-----SGQLEGSGA---AKPPRGAGTGGSGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHS 292
Cdd:cd22538 233 LPPSypdssPSPLAGAGGsmlTGGPTAPLGGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHS 303
SP6-9-like_N cd22547
N-terminal domain of invertebrate transcription factor Specificity Proteins (SP) similar to ...
91-292 4.64e-21

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: 90.93  E-value: 4.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  91 PFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSldmtHPYGSWYKAGIHAGISPGPG----NTPTPWWDMHPGGNWLG 166
Cdd:cd22547  28 PWKKSPPSVSSNSSQASLLQKVHSSVSDSRPVYSH----HPYESWPFNATSHHHKKEEVsssaNNSSSWWDMHSAAGSWL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 167 ggqgqgdglqgTLSTGPAQPPLNPQLPTYP-SDFAPLNPAPYPAPHLLQPGPQhvLPQDVYK---PKAvGNSGQLEGSGA 242
Cdd:cd22547 104 -----------DESSAAATGPHSQISPNYPsSDYSLGHLLASSSAPLLLSGQH--LLQDTYKsmlPSQ-GDIGASSFPSS 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 30913319 243 AKPPRGAGTGGSGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHS 292
Cdd:cd22547 170 LLSQPSLSGVPSPRSQRRYTGRATCDCPNCQEAERLGPAGAHLRKKNIHS 219
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
19-291 6.97e-16

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: 76.88  E-value: 6.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  19 MLTAACSKFGG--SSPLRDSTTLGKGGTKKPYADLSAPKTmgDAYPAPFSSTNGLLSPAGSPPAPASGYANDyppfPHSf 96
Cdd:cd22544   1 MLTAVCGSLGNqhSETPRASPPTLDLQPLQPYQIHSSPEA--GDYPSPLQPTELQSLPLGPGVDFSARESYE----PHS- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319  97 pGPTGAQDPGLLVPKGHSSSDCLPSvytsLDMTHPYGSWYKAGiHAGISPGPGNTPtPWWDMHPGGNWLGGGQGQGDglq 176
Cdd:cd22544  74 -SRRTCLDLESDLPLGPFPKLLHPP----PDMAHPYESWFRPP-HPGGSGEEGGVP-SWWDLHAGSSWMDLQHGQGG--- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319 177 gtLSTGPAQPPLNPQLPTYPSDfaplNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGAAKPPRGAGTGGSGg 256
Cdd:cd22544 144 --LQSPGPPGGLQPPLGGYGSE----HQLCGPPHHLLPPAQHLMGQEGPKLLEHPAEDPSLDGSPRPKGSRRSVPRSSG- 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 30913319 257 yagsgagRSTCDCPNCQELERLGAAAAGLRKKPIH 291
Cdd:cd22544 217 -------QAACRCPNCQEAERLGPPPDGGKKKHLH 244
zf-H2C2_2 pfam13465
Zinc-finger double domain;
337-362 8.29e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 8.29e-06
                          10        20
                  ....*....|....*....|....*.
gi 30913319   337 ELERHVRTHTREKKFTCLLCSKRFTR 362
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
351-373 6.18e-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: 6.18e-05
                          10        20
                  ....*....|....*....|...
gi 30913319   351 FTCLLCSKRFTRSDHLSKHQRTH 373
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
16-247 6.75e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319    16 PLAMLTAACSKFGGSSPLRDSTTLGKGGTKKPYADLSAPKTMgdAYPAPFSSTNGLLSPAGSPPAPASGYAndypPFPHS 95
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSPWDPADPPA----AVLAP 2814
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30913319    96 FPGPTGAQDPGLLVPKGHSSSDCLPSVYTS-LDMTHPYGSWYKAGIHAGISPGPGNTP-TPWWDMHPGGNWLGGGQGQGD 173
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVAPGGDVRRRPPSRSPAaKPAAPARPPVRRLARPAVSRS 2894
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30913319   174 GLQGTLSTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGpqhvLPQDVYKPKAvGNSGQLEGSGAAKPPR 247
Cdd:PHA03247 2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPTT-DPAGAGEPSGAVPQPW 2963
zf-H2C2_2 pfam13465
Zinc-finger double domain;
307-334 9.24e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.24e-05
                          10        20
                  ....*....|....*....|....*...
gi 30913319   307 HLKAHLRWHTGERPFVCNwlFCGKRFTR 334
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 ...
321-345 5.24e-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: 5.24e-04
                          10        20
                  ....*....|....*....|....*
gi 30913319   321 FVCNwlFCGKRFTRSDELERHVRTH 345
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-373 8.04e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 8.04e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30913319 306 SHLKAHLRW--HTGE--RPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLL--CSKRFTRSDHLSKHQRTH 373
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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