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Conserved domains on  [gi|62088936|dbj|BAD92915|]
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Sp1 transcription factor variant, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 1-405 3.55e-106

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.


The actual alignment was detected with superfamily member cd22539:

Pssm-ID: 425404  Cd Length: 433  Bit Score: 325.70  E-value: 3.55e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936   1 NIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAatltpssqavtisssgsqesgsqpvt 78
Cdd:cd22539 170 GNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNITLLPVSSVTA-------------------------- 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  79 sgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnfttsgssgtNSQGQtpqrvsglqgsdaLNIQQNQtsggsl 158
Cdd:cd22539 224 ------------------SFFTNANSYSTTTTTSNMG------------QQQQQ-------------ILIQPQL------ 254

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 159 qagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNTGPIIIRTPtVGPNG 238
Cdd:cd22539 255 -------------------------VQGGQTIQALQAASLPGQTFTTQTISQEALQNLQIQTVPNSGPIIIRTP-VGPNG 308

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 239 QVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltpiasaasipagTVTVNAAQLSSMPGLQTINLSALGTS 318
Cdd:cd22539 309 QVSWQTIQLQNLQ-----------------------------------------TVTVNAAQLSSMPGLQTINLNALGAS 347

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 319 GIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDP 398
Cdd:cd22539 348 GIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDP 426


                ....*..
gi 62088936 399 GKKKQHI 405
Cdd:cd22539 427 GKKKQHI 433
zf-H2C2_2 pfam13465
Zinc-finger double domain;
450-473 6.57e-09

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 6.57e-09
                          10        20
                  ....*....|....*....|....
gi 62088936   450 ELQRHKRTHTGEKKFACPECPKRF 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-447 6.96e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.96e-06
                          10        20
                  ....*....|....*....|....*...
gi 62088936   420 HLRAHLRWHTGERPFMCTwsYCGKRFTR 447
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 ...
 464-486 8.48e-06

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: 8.48e-06
                          10        20
                  ....*....|....*....|...
gi 62088936   464 FACPECPKRFMRSDHLSKHIKTH 486
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 404-428 6.59e-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: 6.59e-03
                          10        20
                  ....*....|....*....|....*
gi 62088936   404 HICHIqgCGKVYGKTSHLRAHLRWH 428
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 ...
 1-405 3.55e-106

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: 325.70  E-value: 3.55e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936   1 NIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAatltpssqavtisssgsqesgsqpvt 78
Cdd:cd22539 170 GNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNITLLPVSSVTA-------------------------- 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  79 sgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnfttsgssgtNSQGQtpqrvsglqgsdaLNIQQNQtsggsl 158
Cdd:cd22539 224 ------------------SFFTNANSYSTTTTTSNMG------------QQQQQ-------------ILIQPQL------ 254

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 159 qagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNTGPIIIRTPtVGPNG 238
Cdd:cd22539 255 -------------------------VQGGQTIQALQAASLPGQTFTTQTISQEALQNLQIQTVPNSGPIIIRTP-VGPNG 308

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 239 QVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltpiasaasipagTVTVNAAQLSSMPGLQTINLSALGTS 318
Cdd:cd22539 309 QVSWQTIQLQNLQ-----------------------------------------TVTVNAAQLSSMPGLQTINLNALGAS 347

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 319 GIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDP 398
Cdd:cd22539 348 GIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDP 426


                ....*..
gi 62088936 399 GKKKQHI 405
Cdd:cd22539 427 GKKKQHI 433
zf-H2C2_2 pfam13465
Zinc-finger double domain;
450-473 6.57e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 6.57e-09
                          10        20
                  ....*....|....*....|....
gi 62088936   450 ELQRHKRTHTGEKKFACPECPKRF 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-447 6.96e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.96e-06
                          10        20
                  ....*....|....*....|....*...
gi 62088936   420 HLRAHLRWHTGERPFMCTwsYCGKRFTR 447
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 ...
 464-486 8.48e-06

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: 8.48e-06
                          10        20
                  ....*....|....*....|...
gi 62088936   464 FACPECPKRFMRSDHLSKHIKTH 486
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
419-490 1.68e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62088936 419 SHLRAHLRW--HTGE--RPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACP--ECPKRFMRSDHLSKHIKTHQNKK 490
Cdd:COG5048 303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
464-486 3.88e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.83  E-value: 3.88e-04
                           10        20
                   ....*....|....*....|...
gi 62088936    464 FACPECPKRFMRSDHLSKHIKTH 486
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
434-458 8.93e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 8.93e-04
                           10        20
                   ....*....|....*....|....*
gi 62088936    434 FMCTWsyCGKRFTRSDELQRHKRTH 458
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 ...
 404-428 6.59e-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: 6.59e-03
                          10        20
                  ....*....|....*....|....*
gi 62088936   404 HICHIqgCGKVYGKTSHLRAHLRWH 428
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 ...
 1-405 3.55e-106

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: 325.70  E-value: 3.55e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936   1 NIIAAMPNLLQQAVPLQ--GLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAatltpssqavtisssgsqesgsqpvt 78
Cdd:cd22539 170 GNIITMPNLLQQAVPIQglGLANNVLPGQTQFVANVPVALNGNITLLPVSSVTA-------------------------- 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  79 sgttissaslvssqasssSFFTNANSYSTTTTTSNMGimnfttsgssgtNSQGQtpqrvsglqgsdaLNIQQNQtsggsl 158
Cdd:cd22539 224 ------------------SFFTNANSYSTTTTTSNMG------------QQQQQ-------------ILIQPQL------ 254

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 159 qagqqkegeqnqqtqqqqiliqpqlVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNTGPIIIRTPtVGPNG 238
Cdd:cd22539 255 -------------------------VQGGQTIQALQAASLPGQTFTTQTISQEALQNLQIQTVPNSGPIIIRTP-VGPNG 308

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 239 QVSWQTLQLQNLQvqnpqaqtitlapmqgvslgqtsssnttltpiasaasipagTVTVNAAQLSSMPGLQTINLSALGTS 318
Cdd:cd22539 309 QVSWQTIQLQNLQ-----------------------------------------TVTVNAAQLSSMPGLQTINLNALGAS 347

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 319 GIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAgGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDP 398
Cdd:cd22539 348 GIQVHQLQGLPLTIANATGEHGAQLGLHGAGGDGLHDDSA-AEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDP 426


                ....*..
gi 62088936 399 GKKKQHI 405
Cdd:cd22539 427 GKKKQHI 433
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 1-405 1.71e-42

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: 161.24  E-value: 1.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936   1 NIIAAmpNLLQQAVPLQ-------GLANNVLSG-QTQYVTNVPVALNGNITLLPVNSVSAA------TLTPSSQAVTISS 66
Cdd:cd22536 197 NIIAQ--NLANQTVPVQirpgvsiPLQLQTIPGaQAQVVTTLPINIGGVTLALPVINNVAAgggsgqLVQPSDGGVSNGN 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  67 SGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTsnmGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDAL 146
Cdd:cd22536 275 QLVSTPITTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSSAET---GQYASTAASSERTEEEPQTSAAESEAQSSSQL 351

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 147 niQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFttQAISQETLQNLQLQAVPNTGP 226
Cdd:cd22536 352 --QSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQPQSFQLQSGQTI--QTIQQQPLQNVQLQAVQSPTQ 427

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 227 IIIRTPTVGPNGQVSWQTLQLQNLQ-VQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAAsIPAGTVTVNAAQLSSMP 305
Cdd:cd22536 428 VLIRAPTLTPSGQISWQTVQVQNIQsLSNLQVQNAGLPQQLTLTPVSSSAGGTTIAQIAPVA-VAGTPITLNAAQLASVP 506

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 306 GLQTINLSALGTSGIQVhpiQGLPLAIANAPGDHGAQLGLH---------GAGGDGIHDDTAGG-----------EEGEN 365
Cdd:cd22536 507 NLQTVNVANLGAAGVQV---QGVPVTITSVAGQQQGQDGVKvqqatiapvTVAVGNIANATIGAvspdqitqvqlQQAQQ 583

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 62088936 366 SPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHI 405
Cdd:cd22536 584 ASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 11-405 5.93e-41

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: 156.26  E-value: 5.93e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  11 QQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATL--TPSSQAVTISSSGSQESGSQPVTSGTTISSASL 88
Cdd:cd22537 184 VVQIQGVSIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLglSGTSQTMTTGITADGQLINTGQAVQSSDNSGES 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  89 VSSQASSSSFFTNANSY-------STTTTTSNMGIMNFTTSGSSGTNSQGQTPQ---RVSGLQGSDALNIQQNQTSGGSL 158
Cdd:cd22537 264 GKVSPDINETNTNADLFvptssssQLPVTIDSTGILQQNASSLTTVSGQVHTSDlqgNYIQAPVSDETQAQNIQVSTAQP 343

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 159 QAGQQKEGEqnqqtqqQQILIQPQLVQGGQALQALQAAplsgQTFTTQAISQETLQNLQLQaVPNTGPIIIRTPTVGPNG 238
Cdd:cd22537 344 SVQQIQLHE-------SQQPTSQAQIVQGITQQAIQGV----QALGAQAIPQQALQNLQLQ-LLNPGTFLIQAQTVTPSG 411

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 239 QVSWQTLQ------LQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPiasaasipagTVTVNAAQlssMPGLQTINL 312
Cdd:cd22537 412 QITWQTFQvqgvqnLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGAITST----------PVSLSTGQ---LPNLQTVTV 478

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 313 SALGTSGIQVHPIQGlplaiANAPGD--------HGAQLGLHGAGGDGIHDDT-----AGGEEGenspDAQPQAGRRTRR 379
Cdd:cd22537 479 NSIDSAGIQLQQSEN-----ADSPADiqikeeepDSEEWQLSGDSTLNTNDLThlrvqLVEEEG----DQPHQEGKRLRR 549

                       410       420
                ....*....|....*....|....*.
gi 62088936 380 EACTCPYCKDSEGRGSgDPGKKKQHI 405
Cdd:cd22537 550 VACTCPNCKEGGGRGS-NLGKKKQHI 574
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 368-405 6.70e-15

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: 69.78  E-value: 6.70e-15
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 62088936 368 DAQPQAGRRTRREACTCPYCKDSEGRGSGDpGKKKQHI 405
Cdd:cd22545  46 DQEPQPGKRLRRVACTCPNCKDGEGRGSED-GKKKQHI 82
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 1-405 3.75e-13

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: 71.88  E-value: 3.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936   1 NIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSG 80
Cdd:cd22540 153 AIITPVQVLQQPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKPS 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936  81 TTISSASLVSSQASSssffTNANSYSTTTTTSNMGIMnfttsGSSGTNsqgqtpqrvsglqgsdaLNIQQNQTSGGSLQA 160
Cdd:cd22540 233 KKIRKKSAQAAQPAV----TVAEQVETVLIETTADNI-----IQAGNN-----------------LLIVQSPGTGQPAVL 286

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 161 GQQKEGEQNQQTQQQQILIqpqlvqggQALQALQAAplsgqTFTTQAISQETLQNLQLQ-AVPNTGPIIIRTPTvgpnGQ 239
Cdd:cd22540 287 QQVQVLQPKQEQQVVQIPQ--------QALRVVQAA-----SATLPTVPQKPLQNIQIQnSEPTPTQVYIKTPS----GE 349

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 240 vsWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIP-----AGTVTVNAAQL-SSMPGLQTINLs 313
Cdd:cd22540 350 --VQTVLLQEAPAATATPSSSTSTVQQQVTANNGTGTSKPNYNVRKERTLPkiapaGGIISLNAAQLaAAAQAIQTINI- 426

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 314 algtSGIQVhpiQGLPLAIANAPGdhGAQLGLHGAGGDGIhddTAGG-------EEGENSPDAQPQAGRRTRREACTCPY 386
Cdd:cd22540 427 ----NGVQV---QGVPVTITNAGG--QQQLTVQTVSSNNL---TISGlsptqiqLQMEQALEIETQPGEKRRRMACTCPN 494

                       410
                ....*....|....*....
gi 62088936 387 CKDSEGRgSGDPGKKKqHI 405
Cdd:cd22540 495 CKDGEKR-SGEQGKKK-HI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
450-473 6.57e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 51.22  E-value: 6.57e-09
                          10        20
                  ....*....|....*....|....
gi 62088936   450 ELQRHKRTHTGEKKFACPECPKRF 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 190-405 1.18e-08

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: 57.34  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 190 LQALQAAPLSG--QTFTTQAISQ-ETLQNLQLQAVPNtgpiiirtptvgPNGQVSWQTLqLQNLQVQNPQAQTITLAPMQ 266
Cdd:cd22553 180 IQAIQSGNAGGgnQALQAQVIPQlAQAAQLQPQQLAQ------------VSSQGYIQQI-PANASQQQPQMVQQGPNQSG 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62088936 267 GVSlGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTI----NLSALGTSGIQVHPIQGLPLAIANAPGDHGAQ 342
Cdd:cd22553 247 QII-GQVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVTSpiqgMTQGLTAPASSSIPTVVQQQAIQGNPLPPGTQ 325

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62088936 343 LGlhgAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDpGKKKQHI 405
Cdd:cd22553 326 II---AAGQQLQQDPNDPTKWQVVADGTPGSKKRLRRVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-447 6.96e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.96e-06
                          10        20
                  ....*....|....*....|....*...
gi 62088936   420 HLRAHLRWHTGERPFMCTwsYCGKRFTR 447
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 ...
 464-486 8.48e-06

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: 8.48e-06
                          10        20
                  ....*....|....*....|...
gi 62088936   464 FACPECPKRFMRSDHLSKHIKTH 486
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 434-458 1.82e-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: 1.82e-05
                          10        20
                  ....*....|....*....|....*
gi 62088936   434 FMCTwsYCGKRFTRSDELQRHKRTH 458
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
419-490 1.68e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62088936 419 SHLRAHLRW--HTGE--RPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACP--ECPKRFMRSDHLSKHIKTHQNKK 490
Cdd:COG5048 303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 464-486 2.00e-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: 2.00e-04
                          10        20
                  ....*....|....*....|...
gi 62088936   464 FACPECPKRFMRSDHLSKHIKTH 486
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
436-490 2.48e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 2.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62088936 436 CTWSYCGKRFTRSDELQRHKRT--HTGE--KKFACPE--CPKRFMRSDHLSKHIKTHQNKK 490
Cdd:COG5048 290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350
ZnF_C2H2 smart00355
zinc finger;
464-486 3.88e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.83  E-value: 3.88e-04
                           10        20
                   ....*....|....*....|...
gi 62088936    464 FACPECPKRFMRSDHLSKHIKTH 486
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
432-490 6.28e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 6.28e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62088936 432 RPFMCtwSYCGKRFTRSDELQRHKRTHTGEKKFAC--PECPKRFMRSDHLSKHIKTHQNKK 490
Cdd:COG5048  32 RPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNP 90
ZnF_C2H2 smart00355
zinc finger;
434-458 8.93e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 8.93e-04
                           10        20
                   ....*....|....*....|....*
gi 62088936    434 FMCTWsyCGKRFTRSDELQRHKRTH 458
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 366-405 1.80e-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: 1.80e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 62088936 366 SPDAQPQAGRRTRReaCTCPYCKDSEGrgSGDPGKKKQHI 405
Cdd:cd22541 108 SPAASLSTTRRCRR--CRCPNCQNPST--SSEPGKKKQHI 143
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
419-484 2.45e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 2.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62088936 419 SHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTgEKKFACPECPKRFMRSDHLSKHIK 484
Cdd:COG5048 402 SNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 434-458 2.46e-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: 2.46e-03
                          10        20
                  ....*....|....*....|....*
gi 62088936   434 FMCTwsYCGKRFTRSDELQRHKRTH 458
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 432-485 4.99e-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: 4.99e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62088936 432 RPFmCtWsYCGKRFtrSDE--LQRHKRTHTgekkFACPECPKRFMRSDHLSKHIKT 485
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 ...
 404-428 6.59e-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: 6.59e-03
                          10        20
                  ....*....|....*....|....*
gi 62088936   404 HICHIqgCGKVYGKTSHLRAHLRWH 428
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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