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Conserved domains on  [gi|289577125|ref|NP_001017371|]
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transcription factor Sp3 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 29-554 0e+00

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: 750.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  29 LASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIP 106
Cdd:cd22537   46 LASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQVIP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 107 QIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVA 186
Cdd:cd22537  126 QIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQVVA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 187 NVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDTDLFVPTS 266
Cdd:cd22537  206 NVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFVPTS 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 267 SSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQ 346
Cdd:cd22537  285 SSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQIVQ 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 347 GITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQVTWQTFQVQGVQNLQNLQIQNTAAQQITLTPV 424
Cdd:cd22537  365 GITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITLTPV 444

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 425 QTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTND 504
Cdd:cd22537  445 QTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLNTND 524

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 289577125 505 LTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 554
Cdd:cd22537  525 LTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
zf-H2C2_2 pfam13465
Zinc-finger double domain;
599-622 1.83e-08

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 1.83e-08
                          10        20
                  ....*....|....*....|....
gi 289577125  599 ELQRHRRTHTGEKKFVCPECSKRF 622
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 583-607 7.15e-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: 43.06  E-value: 7.15e-06
                          10        20
                  ....*....|....*....|....*
gi 289577125  583 FVCNwmYCGKRFTRSDELQRHRRTH 607
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 613-635 7.29e-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: 43.06  E-value: 7.29e-06
                          10        20
                  ....*....|....*....|...
gi 289577125  613 FVCPECSKRFMRSDHLAKHIKTH 635
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-577 8.31e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 8.31e-03
                          10        20
                  ....*....|....*....|....*
gi 289577125  553 HICHIpgCGKVYGKTSHLRAHLRWH 577
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 29-554 0e+00

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: 750.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  29 LASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIP 106
Cdd:cd22537   46 LASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQVIP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 107 QIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVA 186
Cdd:cd22537  126 QIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQVVA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 187 NVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDTDLFVPTS 266
Cdd:cd22537  206 NVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFVPTS 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 267 SSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQ 346
Cdd:cd22537  285 SSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQIVQ 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 347 GITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQVTWQTFQVQGVQNLQNLQIQNTAAQQITLTPV 424
Cdd:cd22537  365 GITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITLTPV 444

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 425 QTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTND 504
Cdd:cd22537  445 QTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLNTND 524

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 289577125 505 LTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 554
Cdd:cd22537  525 LTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
zf-H2C2_2 pfam13465
Zinc-finger double domain;
599-622 1.83e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 1.83e-08
                          10        20
                  ....*....|....*....|....
gi 289577125  599 ELQRHRRTHTGEKKFVCPECSKRF 622
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 583-607 7.15e-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: 43.06  E-value: 7.15e-06
                          10        20
                  ....*....|....*....|....*
gi 289577125  583 FVCNwmYCGKRFTRSDELQRHRRTH 607
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 613-635 7.29e-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: 43.06  E-value: 7.29e-06
                          10        20
                  ....*....|....*....|...
gi 289577125  613 FVCPECSKRFMRSDHLAKHIKTH 635
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
613-635 1.57e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 39.37  E-value: 1.57e-04
                           10        20
                   ....*....|....*....|...
gi 289577125   613 FVCPECSKRFMRSDHLAKHIKTH 635
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
568-650 7.46e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 568 SHLRAHLRW--HSGE--RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHlAKHIKTHQNKKGI 641
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLN-NEPPQSLQQYKDL 381


                 ....*....
gi 289577125 642 HSSSTVLAS 650
Cdd:COG5048  382 KNDKKSETL 390
ZnF_C2H2 smart00355
zinc finger;
583-607 1.17e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.17e-03
                           10        20
                   ....*....|....*....|....*
gi 289577125   583 FVCNWmyCGKRFTRSDELQRHRRTH 607
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 555-632 1.66e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 38.55  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  555 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 627
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....*
gi 289577125  628 LAKHI 632
Cdd:pfam15909  82 LFKHL 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-577 8.31e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 8.31e-03
                          10        20
                  ....*....|....*....|....*
gi 289577125  553 HICHIpgCGKVYGKTSHLRAHLRWH 577
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 29-554 0e+00

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: 750.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  29 LASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAA--TSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIP 106
Cdd:cd22537   46 LASAQLTGAPNRWEVLTPTPTTIKDEAGNLVQIPGGGtvTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQVIP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 107 QIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVA 186
Cdd:cd22537  126 QIQTTDGQQVQLGFATSSDNTGLQQEGGQIQIIPGSNQTIIASGTPSAVQQLLSQSGHVVQIQGVSIGGSSFPGQTQVVA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 187 NVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGeRVSPDINETNTDTDLFVPTS 266
Cdd:cd22537  206 NVPLGLPGNITFVPINSVDLDSLGLSGTSQTMTTGITADGQLINTGQAVQSSDNSGESG-KVSPDINETNTNADLFVPTS 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 267 SSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQ 346
Cdd:cd22537  285 SSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAQIVQ 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 347 GITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQVTWQTFQVQGVQNLQNLQIQNTAAQQITLTPV 424
Cdd:cd22537  365 GITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPAQQITLTPV 444

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 425 QTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTND 504
Cdd:cd22537  445 QTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSENADSPADIQIKEEEPDSEEWQLSGDSTLNTND 524

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 289577125 505 LTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 554
Cdd:cd22537  525 LTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHI 574
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 29-554 3.26e-52

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: 191.28  E-value: 3.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  29 LASAQLGGapNRWEVLSATPTTIKDeaGNLVQIPSAATSSGQYVLPLQN--------------LQNQQIFSVAPGSDSSN 94
Cdd:cd22536   62 LVTTQLAG--NAWQIVAAAPPTSKE--NNVAQQGVSAATSSAAPSSSNNgstsptkvkagnsnASAPGQFQVIQVQNMQN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  95 GTvSSVQYQVIPQIQSADGQQVQIGFTGSSDNGGINQessQIQIIP-GSNQTLLASG--TPSANI--QNLIPQTGQVQVQ 169
Cdd:cd22536  138 PS-GSVQYQVIPQIQTVEGQQIQISPANATALQDLQG---QIQLIPaGNNQAILTTPnrTASGNIiaQNLANQTVPVQIR 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 170 gvaiGGSSFP--------GQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDN- 240
Cdd:cd22536  214 ----PGVSIPlqlqtipgAQAQVVTTLPINIGGVTLALPVINNVAAGGGSGQLVQPSDGGVSNGNQLVSTPITTASVSTm 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 241 --SERTGERVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQsPVSEETQAQNI 318
Cdd:cd22536  290 peSPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASSERTEEEPQTSAAESEAQSSSQLQSNGLQ-NVQDQSNSLQQ 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 319 QVSTAQPVVQHLQLQESQQPTSQAQIVQ------GITPQTIHgvQASGQNIsqqalqNLQLQLNPGTFLIQAQTVTPSGQ 392
Cdd:cd22536  369 VQIVGQPILQQIQIQQPQQQIIQAIQPQsfqlqsGQTIQTIQ--QQPLQNV------QLQAVQSPTQVLIRAPTLTPSGQ 440

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 393 VTWQTFQVQGVQNLQNLQIQNTA-AQQITLTPVQT----LTLGQVAAgGAFTSTPVSLSTGQL---PNLQTVTVNSIDSA 464
Cdd:cd22536  441 ISWQTVQVQNIQSLSNLQVQNAGlPQQLTLTPVSSsaggTTIAQIAP-VAVAGTPITLNAAQLasvPNLQTVNVANLGAA 519

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 465 GIQLHPGENADSPADIRIKEEEPDPEEWQLSGDST-------------LNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVA 531
Cdd:cd22536  520 GVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVTvavgnianatigaVSPDQITQVQLQQAQQASDQEVQPGKRLRRVA 599

                        570       580
                 ....*....|....*....|....
gi 289577125 532 CTCPNCKEGGGRGTN-LGKKKQHI 554
Cdd:cd22536  600 CSCPNCREGEGRGSSePGKKKQHI 623
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 29-554 1.22e-35

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: 140.03  E-value: 1.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  29 LASAQLGGAPNRWEVLSA---TPTTIKDEAGNLVQIPS----AATSSGQYVLPLQNLQNQQIFSVAPGsdssngTVSSVQ 101
Cdd:cd22539   46 LTQAQIAQSANGWQIIPTgsqAPTPSKEQSGDSSTADSskksRVATAGYVVVAAPNLQNQQVLTSLPG------VMPNIQ 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 102 YQVIPQIQSADGQQVQIGFTGSSDNGginQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQ--VQVQGVAIGGSSFP 179
Cdd:cd22539  120 YQVIPQFQTVDGQQLQFATTQAQVQQ---DASGQLQIIPGTNQQIITTNRSGSGNIITMPNLLQqaVPIQGLGLANNVLP 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 180 GQTQVVANVPLGLPGNITFVPINSVdldslglsgssqtmtaginadghlintgqamdssdnsertgervsPDINETNTdt 259
Cdd:cd22539  197 GQTQFVANVPVALNGNITLLPVSSV---------------------------------------------TASFFTNA-- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 260 dlfvptssssqlpvtidstgilqqNTNSLTTSSGQVhssdlqgnyiqspvseetqaqniqvstaqpvvqhlqLQESQQPT 339
Cdd:cd22539  230 ------------------------NSYSTTTTTSNM------------------------------------GQQQQQIL 249

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 340 SQAQIVQGI-TPQTIHGVQASG-----QNISQQALQNLQLQLNPGTFLIQAQT-VTPSGQVTWQTFQVQGVQnlqnlqiq 412
Cdd:cd22539  250 IQPQLVQGGqTIQALQAASLPGqtfttQTISQEALQNLQIQTVPNSGPIIIRTpVGPNGQVSWQTIQLQNLQ-------- 321

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 413 ntaaqqitltpvqtltlgqvaaggafTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENAdsPADIrikEEEPDPEEW 492
Cdd:cd22539  322 --------------------------TVTVNAAQLSSMPGLQTINLNALGASGIQVHQLQGL--PLTI---ANATGEHGA 370

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289577125 493 QLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRG-TNLGKKKQHI 554
Cdd:cd22539  371 QLGLHGAGGDGLHDDSAAEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDsGDPGKKKQHI 433
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 511-554 9.38e-18

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: 78.25  E-value: 9.38e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 289577125 511 QVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 554
Cdd:cd22545   39 QVIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQHI 82
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 56-554 2.26e-12

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: 69.96  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  56 GNLVQIP----SAATSSGQYVLPLQNlqnqqifSVAPGSDSSNGTVSSVQYQVIPQIQSAdgqqvqigftgssdngGINQ 131
Cdd:cd22540   83 GNIIQLQgsqlSSSAPGGQQVFAIQN-------PTMIIKGSQTRSSTNQQYQISPQIQAA----------------GQIN 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 132 ESSQIQIIPGSNQTLLASgTPSANIQNLIPQTGQVQVQGVAIGGSSfPGQTQVVAN-VPLGLPGNITFV-PINSVDLDSl 209
Cdd:cd22540  140 NSGQIQIIPGTNQAIITP-VQVLQQPQQAHKPVPIKPAPLQTSNTN-SASLQVPGNvIKLQSGGNVALTlPVNNLVGTQ- 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 210 glSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDINETNTDTdlfvptssssqlpvtidstgILQQNTNSLt 289
Cdd:cd22540  217 --DGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADN--------------------IIQAGNNLL- 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 290 tssgqvhssdlqgnYIQSPvseetqaqniqvSTAQPVVqhLQLQESQQPTSQAQIVQgITPQTIHGVQASGQN-ISQQAL 368
Cdd:cd22540  274 --------------IVQSP------------GTGQPAV--LQQVQVLQPKQEQQVVQ-IPQQALRVVQAASATlPTVPQK 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 369 QNLQLQLNPGTFL-IQAQTVTPSGQVTWQTFQV-------QGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTS 440
Cdd:cd22540  325 PLQNIQIQNSEPTpTQVYIKTPSGEVQTVLLQEapaatatPSSSTSTVQQQVTANNGTGTSKPNYNVRKERTLPKIAPAG 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 441 TPVSLSTGQLP----NLQTVTVN---------SIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLsgdstlntndlth 507
Cdd:cd22540  405 GIISLNAAQLAaaaqAIQTININgvqvqgvpvTITNAGGQQQLTVQTVSSNNLTISGLSPTQIQLQM------------- 471

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 289577125 508 lrvqvvDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKqHI 554
Cdd:cd22540  472 ------EQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKK-HI 511
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 314-554 1.39e-10

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: 63.89  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 314 QAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTfliqaQTVTPSGQV 393
Cdd:cd22553  193 QALQAQVIPQLAQAAQLQPQQLAQVSSQGYIQQIPANASQQQPQMVQQGPNQSGQIIGQVASASSI-----QAAAIPLTV 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 394 TWQTFQVQGVQNLQNlqiqntaAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVnsIDSAGIQLHPGEN 473
Cdd:cd22553  268 YTGALAGQNGSNQQQ-------VGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQGNPLPPGTQ--IIAAGQQLQQDPN 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 474 adspadirikeeepDPEEWQLSGDSTLNTndlthlrvqvvdeegdqqhqeGKRLRRVACTCPNCKEGGGRGTNLGKKKQH 553
Cdd:cd22553  339 --------------DPTKWQVVADGTPGS---------------------KKRLRRVACTCPNCRDGDGTRNGENKKKQH 383


                 .
gi 289577125 554 I 554
Cdd:cd22553  384 I 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
599-622 1.83e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.45  E-value: 1.83e-08
                          10        20
                  ....*....|....*....|....
gi 289577125  599 ELQRHRRTHTGEKKFVCPECSKRF 622
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 583-607 7.15e-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: 43.06  E-value: 7.15e-06
                          10        20
                  ....*....|....*....|....*
gi 289577125  583 FVCNwmYCGKRFTRSDELQRHRRTH 607
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 613-635 7.29e-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: 43.06  E-value: 7.29e-06
                          10        20
                  ....*....|....*....|...
gi 289577125  613 FVCPECSKRFMRSDHLAKHIKTH 635
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
613-635 1.57e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 39.37  E-value: 1.57e-04
                           10        20
                   ....*....|....*....|...
gi 289577125   613 FVCPECSKRFMRSDHLAKHIKTH 635
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 613-635 4.20e-04

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 38.01  E-value: 4.20e-04
                          10        20
                  ....*....|....*....|...
gi 289577125  613 FVCPECSKRFMRSDHLAKHIKTH 635
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
568-650 7.46e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125 568 SHLRAHLRW--HSGE--RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHlAKHIKTHQNKKGI 641
Cdd:COG5048  303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLN-NEPPQSLQQYKDL 381


                 ....*....
gi 289577125 642 HSSSTVLAS 650
Cdd:COG5048  382 KNDKKSETL 390
ZnF_C2H2 smart00355
zinc finger;
583-607 1.17e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.17e-03
                           10        20
                   ....*....|....*....|....*
gi 289577125   583 FVCNWmyCGKRFTRSDELQRHRRTH 607
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 555-632 1.66e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 38.55  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289577125  555 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 627
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....*
gi 289577125  628 LAKHI 632
Cdd:pfam15909  82 LFKHL 86
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 583-607 6.18e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 6.18e-03
                          10        20
                  ....*....|....*....|....*
gi 289577125  583 FVCNwmYCGKRFTRSDELQRHRRTH 607
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 581-634 8.10e-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: 36.00  E-value: 8.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 289577125 581 RPFvCnWmYCGKRFtrSDE--LQRHRRTHTgekkFVCPECSKRFMRSDHLAKHIKT 634
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 ...
 553-577 8.31e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 8.31e-03
                          10        20
                  ....*....|....*....|....*
gi 289577125  553 HICHIpgCGKVYGKTSHLRAHLRWH 577
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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