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Conserved domains on  [gi|352962149|ref|NP_001238754|]
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transcription factor Sp1 isoform c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 59-579 6.19e-159

N-terminal domain of transcription factor Specificity Protein (SP) 1; 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. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 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 KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


:

Pssm-ID: 411775  Cd Length: 433  Bit Score: 467.07  E-value: 6.19e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149  59 WQIISSSSGATPTSKEQSGSStngsNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQ 138
Cdd:cd22539   58 WQIIPTGSQAPTPSKEQSGDS----STADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 139 LQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNI 216
Cdd:cd22539  134 LQFATTQAQVQQDASGQLQIIPGTNQQIITTNRSGSGNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNI 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 217 TLLPVNSVSAatltpssqavtisssgsqesgsqpvtsgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnftts 296
Cdd:cd22539  214 TLLPVSSVTA--------------------------------------------SFFTNANSYSTTTTTSNMG------- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 297 gssgtNSQGQtpqrvsglqgsdaLNIQQNQtsggslqagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQT 376
Cdd:cd22539  243 -----QQQQQ-------------ILIQPQL-------------------------------VQGGQTIQALQAASLPGQT 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 377 FTTQAISQETLQNLQLQAVPNSGPIIIRTPtVGPNGQVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltp 456
Cdd:cd22539  274 FTTQTISQEALQNLQIQTVPNSGPIIIRTP-VGPNGQVSWQTIQLQNLQ------------------------------- 321

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 457 iasaasipagTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEE 536
Cdd:cd22539  322 ----------TVTVNAAQLSSMPGLQTINLNALGASGIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEE 390

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 352962149 537 GENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHI 579
Cdd:cd22539  391 GETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
zf-H2C2_2 pfam13465
Zinc-finger double domain;
624-647 8.54e-09

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 8.54e-09
                          10        20
                  ....*....|....*....|....
gi 352962149  624 ELQRHKRTHTGEKKFACPECPKRF 647
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
594-621 9.07e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 9.07e-06
                          10        20
                  ....*....|....*....|....*...
gi 352962149  594 HLRAHLRWHTGERPFMCTwsYCGKRFTR 621
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 ...
 638-660 1.10e-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: 42.29  E-value: 1.10e-05
                          10        20
                  ....*....|....*....|...
gi 352962149  638 FACPECPKRFMRSDHLSKHIKTH 660
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 578-602 8.58e-03

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: 34.20  E-value: 8.58e-03
                          10        20
                  ....*....|....*....|....*
gi 352962149  578 HICHIqgCGKVYGKTSHLRAHLRWH 602
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 59-579 6.19e-159

N-terminal domain of transcription factor Specificity Protein (SP) 1; 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. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 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 KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


Pssm-ID: 411775  Cd Length: 433  Bit Score: 467.07  E-value: 6.19e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149  59 WQIISSSSGATPTSKEQSGSStngsNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQ 138
Cdd:cd22539   58 WQIIPTGSQAPTPSKEQSGDS----STADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 139 LQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNI 216
Cdd:cd22539  134 LQFATTQAQVQQDASGQLQIIPGTNQQIITTNRSGSGNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNI 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 217 TLLPVNSVSAatltpssqavtisssgsqesgsqpvtsgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnftts 296
Cdd:cd22539  214 TLLPVSSVTA--------------------------------------------SFFTNANSYSTTTTTSNMG------- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 297 gssgtNSQGQtpqrvsglqgsdaLNIQQNQtsggslqagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQT 376
Cdd:cd22539  243 -----QQQQQ-------------ILIQPQL-------------------------------VQGGQTIQALQAASLPGQT 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 377 FTTQAISQETLQNLQLQAVPNSGPIIIRTPtVGPNGQVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltp 456
Cdd:cd22539  274 FTTQTISQEALQNLQIQTVPNSGPIIIRTP-VGPNGQVSWQTIQLQNLQ------------------------------- 321

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 457 iasaasipagTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEE 536
Cdd:cd22539  322 ----------TVTVNAAQLSSMPGLQTINLNALGASGIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEE 390

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 352962149 537 GENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHI 579
Cdd:cd22539  391 GETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
zf-H2C2_2 pfam13465
Zinc-finger double domain;
624-647 8.54e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 8.54e-09
                          10        20
                  ....*....|....*....|....
gi 352962149  624 ELQRHKRTHTGEKKFACPECPKRF 647
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
594-621 9.07e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 9.07e-06
                          10        20
                  ....*....|....*....|....*...
gi 352962149  594 HLRAHLRWHTGERPFMCTwsYCGKRFTR 621
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 ...
 638-660 1.10e-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: 42.29  E-value: 1.10e-05
                          10        20
                  ....*....|....*....|...
gi 352962149  638 FACPECPKRFMRSDHLSKHIKTH 660
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
593-664 4.29e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 4.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 352962149 593 SHLRAHLRW--HTGE--RPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACP--ECPKRFMRSDHLSKHIKTHQNKK 664
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
638-660 5.05e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.83  E-value: 5.05e-04
                           10        20
                   ....*....|....*....|...
gi 352962149   638 FACPECPKRFMRSDHLSKHIKTH 660
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
608-632 1.16e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.16e-03
                           10        20
                   ....*....|....*....|....*
gi 352962149   608 FMCTWsyCGKRFTRSDELQRHKRTH 632
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 578-602 8.58e-03

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: 34.20  E-value: 8.58e-03
                          10        20
                  ....*....|....*....|....*
gi 352962149  578 HICHIqgCGKVYGKTSHLRAHLRWH 602
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 59-579 6.19e-159

N-terminal domain of transcription factor Specificity Protein (SP) 1; 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. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 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 KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


Pssm-ID: 411775  Cd Length: 433  Bit Score: 467.07  E-value: 6.19e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149  59 WQIISSSSGATPTSKEQSGSStngsNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQ 138
Cdd:cd22539   58 WQIIPTGSQAPTPSKEQSGDS----STADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 139 LQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNI 216
Cdd:cd22539  134 LQFATTQAQVQQDASGQLQIIPGTNQQIITTNRSGSGNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNI 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 217 TLLPVNSVSAatltpssqavtisssgsqesgsqpvtsgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnftts 296
Cdd:cd22539  214 TLLPVSSVTA--------------------------------------------SFFTNANSYSTTTTTSNMG------- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 297 gssgtNSQGQtpqrvsglqgsdaLNIQQNQtsggslqagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQT 376
Cdd:cd22539  243 -----QQQQQ-------------ILIQPQL-------------------------------VQGGQTIQALQAASLPGQT 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 377 FTTQAISQETLQNLQLQAVPNSGPIIIRTPtVGPNGQVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltp 456
Cdd:cd22539  274 FTTQTISQEALQNLQIQTVPNSGPIIIRTP-VGPNGQVSWQTIQLQNLQ------------------------------- 321

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 457 iasaasipagTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEE 536
Cdd:cd22539  322 ----------TVTVNAAQLSSMPGLQTINLNALGASGIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEE 390

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 352962149 537 GENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHI 579
Cdd:cd22539  391 GETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 59-579 8.87e-62

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 218.63  E-value: 8.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149  59 WQIISSssgATPTSKE----QSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLP-GVMPN----IQYQVIP 129
Cdd:cd22536   72 WQIVAA---APPTSKEnnvaQQGVSAATSSAAPSSSNNGSTSPTKVKAGNSNASAPGQFQVIQvQNMQNpsgsVQYQVIP 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 130 QFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQII---TNRGSGGNIIAAmpNLLQQAVPLQ-------GLANNVLS 199
Cdd:cd22536  149 QIQTVEGQQIQISPANATALQDLQGQIQLIPAGNNQAIlttPNRTASGNIIAQ--NLANQTVPVQirpgvsiPLQLQTIP 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 200 G-QTQYVTNVPVALNGNITLLPVNSVSAA------TLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSF 272
Cdd:cd22536  227 GaQAQVVTTLPINIGGVTLALPVINNVAAgggsgqLVQPSDGGVSNGNQLVSTPITTASVSTMPESPSSSTTCTTTASTS 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 273 FTNANSYSTTTTTsnmGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALniQQNQTSGGSLQAGQQKEGEQNQQTQQQQIL 352
Cdd:cd22536  307 LTSSDTLVSSAET---GQYASTAASSERTEEEPQTSAAESEAQSSSQL--QSNGLQNVQDQSNSLQQVQIVGQPILQQIQ 381

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 353 IQPQLVQGGQALQALQAAPLSGQTFttQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQ-VQNPQA 431
Cdd:cd22536  382 IQQPQQQIIQAIQPQSFQLQSGQTI--QTIQQQPLQNVQLQAVQSPTQVLIRAPTLTPSGQISWQTVQVQNIQsLSNLQV 459

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 432 QTITLAPMQGVSLGQTSSSNTTLTPIASAAsIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVhpiQGLPLAIANAPG 511
Cdd:cd22536  460 QNAGLPQQLTLTPVSSSAGGTTIAQIAPVA-VAGTPITLNAAQLASVPNLQTVNVANLGAAGVQV---QGVPVTITSVAG 535

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 512 DHGAQLGLH---------GAGGDGIHDDTAGG-----------EEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGD 571
Cdd:cd22536  536 QQQGQDGVKvqqatiapvTVAVGNIANATIGAvspdqitqvqlQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSE 615


                 ....*...
gi 352962149 572 PGKKKQHI 579
Cdd:cd22536  616 PGKKKQHI 623
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 93-579 9.58e-62

N-terminal domain of transcription factor Specificity Protein (SP) 3; 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. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.


Pssm-ID: 411774 [Multi-domain]  Cd Length: 574  Bit Score: 217.12  E-value: 9.58e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149  93 TVSGGQYVVAAApNLQNQQVLTGLP------GVMPNIQYQVIPQFQTVDGQQLQFAATGAQ---VQQDGSGQIQIIPGAN 163
Cdd:cd22537   84 VTSSGQYVLPLQ-SLQNQQIFSVAPgsdasnGTVPNVQYQVIPQIQTTDGQQVQLGFATSSdntGLQQEGGQIQIIPGSN 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 164 QQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATL--TPSSQAVTISSS 241
Cdd:cd22537  163 QTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLglSGTSQTMTTGIT 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 242 GSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSY-------STTTTTSNMGIMNFTTSGSSGTNSQGQTPQ---RV 311
Cdd:cd22537  243 ADGQLINTGQAVQSSDNSGESGKVSPDINETNTNADLFvptssssQLPVTIDSTGILQQNASSLTTVSGQVHTSDlqgNY 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 312 SGLQGSDALNIQQNQTSGGSLQAGQQKEGEqnqqtqqQQILIQPQLVQGGQALQALQAAplsgQTFTTQAISQETLQNLQ 391
Cdd:cd22537  323 IQAPVSDETQAQNIQVSTAQPSVQQIQLHE-------SQQPTSQAQIVQGITQQAIQGV----QALGAQAIPQQALQNLQ 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 392 LQaVPNSGPIIIRTPTVGPNGQVSWQTLQ------LQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPiasaasipa 465
Cdd:cd22537  392 LQ-LLNPGTFLIQAQTVTPSGQITWQTFQvqgvqnLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGAITST--------- 461

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 466 gTVTVNAAQlssMPGLQTINLSALGTSGIQVHPIQGlplaiANAPGD--------HGAQLGLHGAGGDGIHDDT-AGGEE 536
Cdd:cd22537  462 -PVSLSTGQ---LPNLQTVTVNSIDSAGIQLQQSEN-----ADSPADiqikeeepDSEEWQLSGDSTLNTNDLThLRVQL 532

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 352962149 537 GENSPDAQPQAGRRTRREACTCPYCKDSEGRGSgDPGKKKQHI 579
Cdd:cd22537  533 VEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGS-NLGKKKQHI 574
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 122-579 1.14e-19

N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 93.07  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 122 NIQYQVIPQFQtvdgqqlqfaatgAQVQQDGSGQIQIIPGANQQIITNRgsggnIIAAMPNLLQQAVPLQglannVLSGQ 201
Cdd:cd22540  123 NQQYQISPQIQ-------------AAGQINNSGQIQIIPGTNQAIITPV-----QVLQQPQQAHKPVPIK-----PAPLQ 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 202 TQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLvssqassssfftNANSYST 281
Cdd:cd22540  180 TSNTNSASLQVPGNVIKLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKKSA------------QAAQPAV 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 282 TTTTSNMGIMNFTTSGSSGtnsqgqtpqrvsglQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIqpqlvqgg 361
Cdd:cd22540  248 TVAEQVETVLIETTADNII--------------QAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQ-------- 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 362 QALQALQAAplsgqTFTTQAISQETLQNLQLQ-AVPNSGPIIIRTPTvgpnGQvsWQTLQLQNLQVQNPQAQTITLAPMQ 440
Cdd:cd22540  306 QALRVVQAA-----SATLPTVPQKPLQNIQIQnSEPTPTQVYIKTPS----GE--VQTVLLQEAPAATATPSSSTSTVQQ 374

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 441 GVSLGQTSSSNTTLTPIASAASIP-----AGTVTVNAAQL-SSMPGLQTINLSalgtsGIQVhpiQGLPLAIANAPGdhG 514
Cdd:cd22540  375 QVTANNGTGTSKPNYNVRKERTLPkiapaGGIISLNAAQLaAAAQAIQTININ-----GVQV---QGVPVTITNAGG--Q 444

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 352962149 515 AQLGLHGAGGDGIhddTAGG-------EEGENSPDAQPQAGRRTRREACTCPYCKDSEGRgSGDPGKKKqHI 579
Cdd:cd22540  445 QQLTVQTVSSNNL---TISGlsptqiqLQMEQALEIETQPGEKRRRMACTCPNCKDGEKR-SGEQGKKK-HI 511
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 542-579 1.34e-14

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 69.40  E-value: 1.34e-14
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 352962149 542 DAQPQAGRRTRREACTCPYCKDSEGRGSGDpGKKKQHI 579
Cdd:cd22545   46 DQEPQPGKRLRRVACTCPNCKDGEGRGSED-GKKKQHI 82
zf-H2C2_2 pfam13465
Zinc-finger double domain;
624-647 8.54e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 8.54e-09
                          10        20
                  ....*....|....*....|....
gi 352962149  624 ELQRHKRTHTGEKKFACPECPKRF 647
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 364-579 1.29e-07

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; 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. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 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. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 54.65  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 364 LQALQAAPLSGQTFTTQA-----ISQETLQNLQLQAVPNSGPIIIRTPTVGpngqvswQTLQLQNLQVQNPQAQTITlap 438
Cdd:cd22553  180 IQAIQSGNAGGGNQALQAqvipqLAQAAQLQPQQLAQVSSQGYIQQIPANA-------SQQQPQMVQQGPNQSGQII--- 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 352962149 439 MQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSgiQVHPIQGLPLAIANAPGDHGAQLG 518
Cdd:cd22553  250 GQVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVTSPIQGMTQGLTAPAS--SSIPTVVQQQAIQGNPLPPGTQII 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 352962149 519 lhgAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDpGKKKQHI 579
Cdd:cd22553  328 ---AAGQQLQQDPNDPTKWQVVADGTPGSKKRLRRVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
594-621 9.07e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 9.07e-06
                          10        20
                  ....*....|....*....|....*...
gi 352962149  594 HLRAHLRWHTGERPFMCTwsYCGKRFTR 621
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 ...
 638-660 1.10e-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: 42.29  E-value: 1.10e-05
                          10        20
                  ....*....|....*....|...
gi 352962149  638 FACPECPKRFMRSDHLSKHIKTH 660
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 608-632 2.37e-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: 41.52  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|....*
gi 352962149  608 FMCTwsYCGKRFTRSDELQRHKRTH 632
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 638-660 2.60e-04

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 38.78  E-value: 2.60e-04
                          10        20
                  ....*....|....*....|...
gi 352962149  638 FACPECPKRFMRSDHLSKHIKTH 660
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
593-664 4.29e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 4.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 352962149 593 SHLRAHLRW--HTGE--RPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACP--ECPKRFMRSDHLSKHIKTHQNKK 664
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
638-660 5.05e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.83  E-value: 5.05e-04
                           10        20
                   ....*....|....*....|...
gi 352962149   638 FACPECPKRFMRSDHLSKHIKTH 660
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
610-664 6.49e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 6.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 352962149 610 CTWSYCGKRFTRSDELQRHKRT--HTGE--KKFACPE--CPKRFMRSDHLSKHIKTHQNKK 664
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350
ZnF_C2H2 smart00355
zinc finger;
608-632 1.16e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.16e-03
                           10        20
                   ....*....|....*....|....*
gi 352962149   608 FMCTWsyCGKRFTRSDELQRHKRTH 632
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
606-664 1.55e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 352962149 606 RPFMCtwSYCGKRFTRSDELQRHKRTHTGEKKFAC--PECPKRFMRSDHLSKHIKTHQNKK 664
Cdd:COG5048   32 RPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNP 90
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 540-579 2.26e-03

N-terminal domain of transcription factor Specificity Protein (SP) 5; 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. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 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 SP5.


Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 39.08  E-value: 2.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 352962149 540 SPDAQPQAGRRTRReaCTCPYCKDSEGrgSGDPGKKKQHI 579
Cdd:cd22541  108 SPAASLSTTRRCRR--CRCPNCQNPST--SSEPGKKKQHI 143
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 608-632 3.21e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.70  E-value: 3.21e-03
                          10        20
                  ....*....|....*....|....*
gi 352962149  608 FMCTwsYCGKRFTRSDELQRHKRTH 632
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
593-658 5.70e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 5.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 352962149 593 SHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTgEKKFACPECPKRFMRSDHLSKHIK 658
Cdd:COG5048  402 SNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 606-659 6.62e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 6.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 352962149 606 RPFmCtWsYCGKRFtrSDE--LQRHKRTHTgekkFACPECPKRFMRSDHLSKHIKT 659
Cdd:cd20908    1 KPW-C-Y-YCDREF--DDEkiLIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 578-602 8.58e-03

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: 34.20  E-value: 8.58e-03
                          10        20
                  ....*....|....*....|....*
gi 352962149  578 HICHIqgCGKVYGKTSHLRAHLRWH 602
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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