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Conserved domains on  [gi|218751903|ref|NP_003100|]
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transcription factor Sp1 isoform b [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 ...
 47-620 0e+00

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: 535.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSStngsNG 126
Cdd:cd22539    5 QESQPSPLALLAATCSRIESPNENSNSSQQQQQQQGELELDLTQAQIAQSANGWQIIPTGSQAPTPSKEQSGDS----ST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 127 SESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQ 206
Cdd:cd22539   81 ADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQLQIIPGTNQQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 207 IITNRGSGGNIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAatltpssqavtisssgs 284
Cdd:cd22539  161 IITTNRSGSGNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNITLLPVSSVTA----------------- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 285 qesgsqpvtsgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnfttsgssgtNSQGQtpqrvsglqgsdaLNIQ 364
Cdd:cd22539  224 ---------------------------SFFTNANSYSTTTTTSNMG------------QQQQQ-------------ILIQ 251

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 365 QNQtsggslqagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIII 444
Cdd:cd22539  252 PQL-------------------------------VQGGQTIQALQAASLPGQTFTTQTISQEALQNLQIQTVPNSGPIII 300

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 445 RTPtVGPNGQVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltpiasaasipagTVTVNAAQLSSMPGLQT 524
Cdd:cd22539  301 RTP-VGPNGQVSWQTIQLQNLQ-----------------------------------------TVTVNAAQLSSMPGLQT 338

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 525 INLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEEGENSPDAQPQAGRRTRREACTCPYCKD 604
Cdd:cd22539  339 INLNALGASGIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEEGETEPDPQPQPGRRTRREACTCPYCKD 417

                        570
                 ....*....|....*.
gi 218751903 605 SEGRGSGDPGKKKQHI 620
Cdd:cd22539  418 GEGRDSGDPGKKKQHI 433
zf-H2C2_2 pfam13465
Zinc-finger double domain;
665-688 9.01e-09

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 9.01e-09
                          10        20
                  ....*....|....*....|....
gi 218751903  665 ELQRHKRTHTGEKKFACPECPKRF 688
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
635-662 9.56e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 9.56e-06
                          10        20
                  ....*....|....*....|....*...
gi 218751903  635 HLRAHLRWHTGERPFMCTwsYCGKRFTR 662
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 ...
 679-701 1.16e-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: 1.16e-05
                          10        20
                  ....*....|....*....|...
gi 218751903  679 FACPECPKRFMRSDHLSKHIKTH 701
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 619-643 9.05e-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: 9.05e-03
                          10        20
                  ....*....|....*....|....*
gi 218751903  619 HICHIqgCGKVYGKTSHLRAHLRWH 643
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 ...
 47-620 0e+00

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: 535.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSStngsNG 126
Cdd:cd22539    5 QESQPSPLALLAATCSRIESPNENSNSSQQQQQQQGELELDLTQAQIAQSANGWQIIPTGSQAPTPSKEQSGDS----ST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 127 SESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQ 206
Cdd:cd22539   81 ADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQLQIIPGTNQQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 207 IITNRGSGGNIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAatltpssqavtisssgs 284
Cdd:cd22539  161 IITTNRSGSGNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNITLLPVSSVTA----------------- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 285 qesgsqpvtsgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnfttsgssgtNSQGQtpqrvsglqgsdaLNIQ 364
Cdd:cd22539  224 ---------------------------SFFTNANSYSTTTTTSNMG------------QQQQQ-------------ILIQ 251

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 365 QNQtsggslqagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIII 444
Cdd:cd22539  252 PQL-------------------------------VQGGQTIQALQAASLPGQTFTTQTISQEALQNLQIQTVPNSGPIII 300

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 445 RTPtVGPNGQVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltpiasaasipagTVTVNAAQLSSMPGLQT 524
Cdd:cd22539  301 RTP-VGPNGQVSWQTIQLQNLQ-----------------------------------------TVTVNAAQLSSMPGLQT 338

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 525 INLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEEGENSPDAQPQAGRRTRREACTCPYCKD 604
Cdd:cd22539  339 INLNALGASGIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEEGETEPDPQPQPGRRTRREACTCPYCKD 417

                        570
                 ....*....|....*.
gi 218751903 605 SEGRGSGDPGKKKQHI 620
Cdd:cd22539  418 GEGRDSGDPGKKKQHI 433
zf-H2C2_2 pfam13465
Zinc-finger double domain;
665-688 9.01e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 9.01e-09
                          10        20
                  ....*....|....*....|....
gi 218751903  665 ELQRHKRTHTGEKKFACPECPKRF 688
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
635-662 9.56e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 9.56e-06
                          10        20
                  ....*....|....*....|....*...
gi 218751903  635 HLRAHLRWHTGERPFMCTwsYCGKRFTR 662
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 ...
 679-701 1.16e-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: 1.16e-05
                          10        20
                  ....*....|....*....|...
gi 218751903  679 FACPECPKRFMRSDHLSKHIKTH 701
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
679-701 5.32e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.83  E-value: 5.32e-04
                           10        20
                   ....*....|....*....|...
gi 218751903   679 FACPECPKRFMRSDHLSKHIKTH 701
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
634-705 8.04e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 8.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218751903 634 SHLRAHLRW--HTGE--RPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACP--ECPKRFMRSDHLSKHIKTHQNKK 705
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
649-673 1.23e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.23e-03
                           10        20
                   ....*....|....*....|....*
gi 218751903   649 FMCTWsyCGKRFTRSDELQRHKRTH 673
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 ...
 619-643 9.05e-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: 9.05e-03
                          10        20
                  ....*....|....*....|....*
gi 218751903  619 HICHIqgCGKVYGKTSHLRAHLRWH 643
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 ...
 47-620 0e+00

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: 535.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSStngsNG 126
Cdd:cd22539    5 QESQPSPLALLAATCSRIESPNENSNSSQQQQQQQGELELDLTQAQIAQSANGWQIIPTGSQAPTPSKEQSGDS----ST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 127 SESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQ 206
Cdd:cd22539   81 ADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQLQIIPGTNQQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 207 IITNRGSGGNIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAatltpssqavtisssgs 284
Cdd:cd22539  161 IITTNRSGSGNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNITLLPVSSVTA----------------- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 285 qesgsqpvtsgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnfttsgssgtNSQGQtpqrvsglqgsdaLNIQ 364
Cdd:cd22539  224 ---------------------------SFFTNANSYSTTTTTSNMG------------QQQQQ-------------ILIQ 251

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 365 QNQtsggslqagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIII 444
Cdd:cd22539  252 PQL-------------------------------VQGGQTIQALQAASLPGQTFTTQTISQEALQNLQIQTVPNSGPIII 300

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 445 RTPtVGPNGQVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltpiasaasipagTVTVNAAQLSSMPGLQT 524
Cdd:cd22539  301 RTP-VGPNGQVSWQTIQLQNLQ-----------------------------------------TVTVNAAQLSSMPGLQT 338

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 525 INLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEEGENSPDAQPQAGRRTRREACTCPYCKD 604
Cdd:cd22539  339 INLNALGASGIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEEGETEPDPQPQPGRRTRREACTCPYCKD 417

                        570
                 ....*....|....*.
gi 218751903 605 SEGRGSGDPGKKKQHI 620
Cdd:cd22539  418 GEGRDSGDPGKKKQHI 433
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 47-620 1.14e-73

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: 250.64  E-value: 1.14e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATptsKEQSGSSTNGSNG 126
Cdd:cd22537    5 QDTQPSPLALLAATCSKIGSPSPGDDAAAAGNAASAGQTGDLASAQLTGAPNRWEVLTPTPTTI---KDEAGNLVQIPGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 127 SESSknrtvSGGQYVVAAApNLQNQQVLTGLP------GVMPNIQYQVIPQFQTVDGQQLQFAATGAQ---VQQDGSGQI 197
Cdd:cd22537   82 GTVT-----SSGQYVLPLQ-SLQNQQIFSVAPgsdasnGTVPNVQYQVIPQIQTTDGQQVQLGFATSSdntGLQQEGGQI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 198 QIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATL--TPSSQ 275
Cdd:cd22537  156 QIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLglSGTSQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 276 AVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSY-------STTTTTSNMGIMNFTTSGSSGTNSQGQT 348
Cdd:cd22537  236 TMTTGITADGQLINTGQAVQSSDNSGESGKVSPDINETNTNADLFvptssssQLPVTIDSTGILQQNASSLTTVSGQVHT 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 349 PQ---RVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEqnqqtqqQQILIQPQLVQGGQALQALQAAplsgQTFTTQAISQ 425
Cdd:cd22537  316 SDlqgNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHE-------SQQPTSQAQIVQGITQQAIQGV----QALGAQAIPQ 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 426 ETLQNLQLQaVPNSGPIIIRTPTVGPNGQVSWQTLQ------LQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPia 499
Cdd:cd22537  385 QALQNLQLQ-LLNPGTFLIQAQTVTPSGQITWQTFQvqgvqnLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGAITST-- 461

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 500 saasipagTVTVNAAQlssMPGLQTINLSALGTSGIQVHPIQGlplaiANAPGD--------HGAQLGLHGAGGDGIHDD 571
Cdd:cd22537  462 --------PVSLSTGQ---LPNLQTVTVNSIDSAGIQLQQSEN-----ADSPADiqikeeepDSEEWQLSGDSTLNTNDL 525

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|
gi 218751903 572 T-AGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSgDPGKKKQHI 620
Cdd:cd22537  526 ThLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGS-NLGKKKQHI 574
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 47-620 1.58e-72

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: 248.68  E-value: 1.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQG------PSQ-----SGGTGELDLTATQLSqgANGWQIISSssgATPTSKE 115
Cdd:cd22536   10 QDSQPSPLALLAATCSKIGTPGENQGAGQQqqiiidPSQglvqlQNQPQQLELVTTQLA--GNAWQIVAA---APPTSKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 116 ----QSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLP-GVMPN----IQYQVIPQFQTVDGQQLQFAATG 186
Cdd:cd22536   85 nnvaQQGVSAATSSAAPSSSNNGSTSPTKVKAGNSNASAPGQFQVIQvQNMQNpsgsVQYQVIPQIQTVEGQQIQISPAN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 187 AQVQQDGSGQIQIIPGANQQII---TNRGSGGNIIAAmpNLLQQAVPLQ-------GLANNVLSG-QTQYVTNVPVALNG 255
Cdd:cd22536  165 ATALQDLQGQIQLIPAGNNQAIlttPNRTASGNIIAQ--NLANQTVPVQirpgvsiPLQLQTIPGaQAQVVTTLPINIGG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 256 NITLLPVNSVSAA------TLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTsnm 329
Cdd:cd22536  243 VTLALPVINNVAAgggsgqLVQPSDGGVSNGNQLVSTPITTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSSAET--- 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 330 GIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALniQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQ 409
Cdd:cd22536  320 GQYASTAASSERTEEEPQTSAAESEAQSSSQL--QSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQPQS 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 410 AAPLSGQTFttQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQ-VQNPQAQTITLAPMQGVSLGQT 488
Cdd:cd22536  398 FQLQSGQTI--QTIQQQPLQNVQLQAVQSPTQVLIRAPTLTPSGQISWQTVQVQNIQsLSNLQVQNAGLPQQLTLTPVSS 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 489 SSSNTTLTPIASAAsIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVhpiQGLPLAIANAPGDHGAQLGLH------- 561
Cdd:cd22536  476 SAGGTTIAQIAPVA-VAGTPITLNAAQLASVPNLQTVNVANLGAAGVQV---QGVPVTITSVAGQQQGQDGVKvqqatia 551

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218751903 562 --GAGGDGIHDDTAGG-----------EEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHI 620
Cdd:cd22536  552 pvTVAVGNIANATIGAvspdqitqvqlQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 47-620 1.05e-24

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: 108.86  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQ---LSQGANGWQIISSSSGATPTSKEQSGSSTNG 123
Cdd:cd22540   20 QDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAplpLGPGKNSIGFLSAKGNIIQLQGSQLSSSAPG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 124 SNGSESSKNRTvsggqYVVAAAPNLQNQqvltglpgvmpNIQYQVIPQFQtvdgqqlqfaatgAQVQQDGSGQIQIIPGA 203
Cdd:cd22540  100 GQQVFAIQNPT-----MIIKGSQTRSST-----------NQQYQISPQIQ-------------AAGQINNSGQIQIIPGT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 204 NQQIITNRgsggnIIAAMPNLLQQAVPLQglannVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSG 283
Cdd:cd22540  151 NQAIITPV-----QVLQQPQQAHKPVPIK-----PAPLQTSNTNSASLQVPGNVIKLQSGGNVALTLPVNNLVGTQDGAT 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 284 SQESGSQPVTSGTTISSASLvssqassssfftNANSYSTTTTTSNMGIMNFTTSGSSGtnsqgqtpqrvsglQGSDALNI 363
Cdd:cd22540  221 QLQLAAAPSKPSKKIRKKSA------------QAAQPAVTVAEQVETVLIETTADNII--------------QAGNNLLI 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 364 QQNQTSGGSLQAGQQKEGEQNQQTQQQQILIqpqlvqggQALQALQAAplsgqTFTTQAISQETLQNLQLQ-AVPNSGPI 442
Cdd:cd22540  275 VQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQ--------QALRVVQAA-----SATLPTVPQKPLQNIQIQnSEPTPTQV 341

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 443 IIRTPTvgpnGQvsWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIP-----AGTVTVNAAQL- 516
Cdd:cd22540  342 YIKTPS----GE--VQTVLLQEAPAATATPSSSTSTVQQQVTANNGTGTSKPNYNVRKERTLPkiapaGGIISLNAAQLa 415

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 517 SSMPGLQTINLsalgtSGIQVhpiQGLPLAIANAPGdhGAQLGLHGAGGDGIhddTAGG-------EEGENSPDAQPQAG 589
Cdd:cd22540  416 AAAQAIQTINI-----NGVQV---QGVPVTITNAGG--QQQLTVQTVSSNNL---TISGlsptqiqLQMEQALEIETQPG 482

                        570       580       590
                 ....*....|....*....|....*....|.
gi 218751903 590 RRTRREACTCPYCKDSEGRgSGDPGKKKqHI 620
Cdd:cd22540  483 EKRRRMACTCPNCKDGEKR-SGEQGKKK-HI 511
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 583-620 2.49e-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: 68.62  E-value: 2.49e-14
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 218751903 583 DAQPQAGRRTRREACTCPYCKDSEGRGSGDpGKKKQHI 620
Cdd:cd22545   46 DQEPQPGKRLRRVACTCPNCKDGEGRGSED-GKKKQHI 82
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 47-76 6.32e-09

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: 53.22  E-value: 6.32e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 218751903  47 QESQPSPLALLAATCSRIESPNENSNNSQG 76
Cdd:cd22545    5 QDSQPSPLALLAATCSKIGSPAENSTGPGG 34
zf-H2C2_2 pfam13465
Zinc-finger double domain;
665-688 9.01e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 9.01e-09
                          10        20
                  ....*....|....*....|....
gi 218751903  665 ELQRHKRTHTGEKKFACPECPKRF 688
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 405-620 3.04e-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: 53.49  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 405 LQALQAAPLSGQTFTTQA-----ISQETLQNLQLQAVPNSGPIIIRTPTVGpngqvswQTLQLQNLQVQNPQAQTITlap 479
Cdd:cd22553  180 IQAIQSGNAGGGNQALQAqvipqLAQAAQLQPQQLAQVSSQGYIQQIPANA-------SQQQPQMVQQGPNQSGQII--- 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218751903 480 MQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSgiQVHPIQGLPLAIANAPGDHGAQLG 559
Cdd:cd22553  250 GQVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVTSPIQGMTQGLTAPAS--SSIPTVVQQQAIQGNPLPPGTQII 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218751903 560 lhgAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDpGKKKQHI 620
Cdd:cd22553  328 ---AAGQQLQQDPNDPTKWQVVADGTPGSKKRLRRVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
635-662 9.56e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 9.56e-06
                          10        20
                  ....*....|....*....|....*...
gi 218751903  635 HLRAHLRWHTGERPFMCTwsYCGKRFTR 662
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 ...
 679-701 1.16e-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: 1.16e-05
                          10        20
                  ....*....|....*....|...
gi 218751903  679 FACPECPKRFMRSDHLSKHIKTH 701
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 649-673 2.50e-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: 2.50e-05
                          10        20
                  ....*....|....*....|....*
gi 218751903  649 FMCTwsYCGKRFTRSDELQRHKRTH 673
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.
 679-701 2.74e-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: 2.74e-04
                          10        20
                  ....*....|....*....|...
gi 218751903  679 FACPECPKRFMRSDHLSKHIKTH 701
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
ZnF_C2H2 smart00355
zinc finger;
679-701 5.32e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.83  E-value: 5.32e-04
                           10        20
                   ....*....|....*....|...
gi 218751903   679 FACPECPKRFMRSDHLSKHIKTH 701
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
634-705 8.04e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 8.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218751903 634 SHLRAHLRW--HTGE--RPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACP--ECPKRFMRSDHLSKHIKTHQNKK 705
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
649-673 1.23e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.23e-03
                           10        20
                   ....*....|....*....|....*
gi 218751903   649 FMCTWsyCGKRFTRSDELQRHKRTH 673
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
651-705 1.25e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218751903 651 CTWSYCGKRFTRSDELQRHKRT--HTGE--KKFACPE--CPKRFMRSDHLSKHIKTHQNKK 705
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
647-705 2.78e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218751903 647 RPFMCtwSYCGKRFTRSDELQRHKRTHTGEKKFAC--PECPKRFMRSDHLSKHIKTHQNKK 705
Cdd:COG5048   32 RPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNP 90
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 581-620 3.13e-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: 38.70  E-value: 3.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 218751903 581 SPDAQPQAGRRTRReaCTCPYCKDSEGrgSGDPGKKKQHI 620
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.
 649-673 3.38e-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: 3.38e-03
                          10        20
                  ....*....|....*....|....*
gi 218751903  649 FMCTwsYCGKRFTRSDELQRHKRTH 673
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 647-700 7.01e-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: 7.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 218751903 647 RPFmCtWsYCGKRFtrSDE--LQRHKRTHTgekkFACPECPKRFMRSDHLSKHIKT 700
Cdd:cd20908    1 KPW-C-Y-YCDREF--DDEkiLIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
634-699 8.98e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 8.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218751903 634 SHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTgEKKFACPECPKRFMRSDHLSKHIK 699
Cdd:COG5048  402 SNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 619-643 9.05e-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: 9.05e-03
                          10        20
                  ....*....|....*....|....*
gi 218751903  619 HICHIqgCGKVYGKTSHLRAHLRWH 643
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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