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Conserved domains on  [gi|1030311313|ref|NP_001313472|]
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transcription factor Sp4 isoform 3 [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 ...
 1-335 2.79e-143

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 cd22536:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 623  Bit Score: 423.94  E-value: 2.79e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313   1 MPESPSSSTTCTTTASTSLTSSDTLVSSADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSL 80
Cdd:cd22536   289 MPESPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313  81 QQVQIVGQPILQQIQIQQPQQQIIQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTV 159
Cdd:cd22536   367 QQVQIVGQPILQQIQIQQPQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTV 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 160 QVQNIQSLSNLQVQNAGLSQQLTITPVSSS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGV 238
Cdd:cd22536   447 QVQNIQSLSNLQVQNAGLPQQLTLTPVSSSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGV 526

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 239 PVTITSVAGQQQGQDGVKVQQATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCR 318
Cdd:cd22536   527 PVTITSVAGQQQGQDGVKVQQATIAPVTVAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCR 606

                         330
                  ....*....|....*..
gi 1030311313 319 EGEGRGSNEPGKKKQHI 335
Cdd:cd22536   607 EGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-403 9.10e-09

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 9.10e-09
                          10        20
                  ....*....|....*....|....
gi 1030311313 380 ELQRHRRTHTGEKRFECPECSKRF 403
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 1.59e-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: 1.59e-05
                          10        20
                  ....*....|....*....|...
gi 1030311313 394 FECPECSKRFMRSDHLSKHVKTH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 364-388 2.95e-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: 40.75  E-value: 2.95e-05
                          10        20
                  ....*....|....*....|....*
gi 1030311313 364 FICNwmFCGKRFTRSDELQRHRRTH 388
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 ...
 334-358 5.54e-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: 5.54e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311313 334 HICHIegCGKVYGKTSHLRAHLRWH 358
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 1-335 2.79e-143

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: 423.94  E-value: 2.79e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313   1 MPESPSSSTTCTTTASTSLTSSDTLVSSADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSL 80
Cdd:cd22536   289 MPESPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313  81 QQVQIVGQPILQQIQIQQPQQQIIQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTV 159
Cdd:cd22536   367 QQVQIVGQPILQQIQIQQPQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTV 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 160 QVQNIQSLSNLQVQNAGLSQQLTITPVSSS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGV 238
Cdd:cd22536   447 QVQNIQSLSNLQVQNAGLPQQLTLTPVSSSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGV 526

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 239 PVTITSVAGQQQGQDGVKVQQATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCR 318
Cdd:cd22536   527 PVTITSVAGQQQGQDGVKVQQATIAPVTVAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCR 606

                         330
                  ....*....|....*..
gi 1030311313 319 EGEGRGSNEPGKKKQHI 335
Cdd:cd22536   607 EGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-403 9.10e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 9.10e-09
                          10        20
                  ....*....|....*....|....
gi 1030311313 380 ELQRHRRTHTGEKRFECPECSKRF 403
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 1.59e-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: 1.59e-05
                          10        20
                  ....*....|....*....|...
gi 1030311313 394 FECPECSKRFMRSDHLSKHVKTH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-420 2.04e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030311313 349 SHLRAHLRW--HTGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHVKTHQNKK 420
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 364-388 2.95e-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: 40.75  E-value: 2.95e-05
                          10        20
                  ....*....|....*....|....*
gi 1030311313 364 FICNwmFCGKRFTRSDELQRHRRTH 388
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
350-377 6.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 6.52e-05
                          10        20
                  ....*....|....*....|....*...
gi 1030311313 350 HLRAHLRWHTGERPFICnwMFCGKRFTR 377
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
394-416 4.21e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 4.21e-04
                           10        20
                   ....*....|....*....|...
gi 1030311313  394 FECPECSKRFMRSDHLSKHVKTH 416
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
364-388 2.08e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.08e-03
                           10        20
                   ....*....|....*....|....*
gi 1030311313  364 FICNWmfCGKRFTRSDELQRHRRTH 388
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 ...
 334-358 5.54e-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: 5.54e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311313 334 HICHIegCGKVYGKTSHLRAHLRWH 358
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 1-335 2.79e-143

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: 423.94  E-value: 2.79e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313   1 MPESPSSSTTCTTTASTSLTSSDTLVSSADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSL 80
Cdd:cd22536   289 MPESPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313  81 QQVQIVGQPILQQIQIQQPQQQIIQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTV 159
Cdd:cd22536   367 QQVQIVGQPILQQIQIQQPQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTV 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 160 QVQNIQSLSNLQVQNAGLSQQLTITPVSSS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGV 238
Cdd:cd22536   447 QVQNIQSLSNLQVQNAGLPQQLTLTPVSSSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGV 526

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 239 PVTITSVAGQQQGQDGVKVQQATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCR 318
Cdd:cd22536   527 PVTITSVAGQQQGQDGVKVQQATIAPVTVAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCR 606

                         330
                  ....*....|....*..
gi 1030311313 319 EGEGRGSNEPGKKKQHI 335
Cdd:cd22536   607 EGEGRGSSEPGKKKQHI 623
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 25-335 1.48e-39

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: 150.48  E-value: 1.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313  25 LVSSADTGQYASTSASSSERTIEESQTPAATESEAQS---SSQLQPNGMQNAQDQSNSLQQVQIVgqpilqqiqiqqpqq 101
Cdd:cd22537   299 LQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNiqvSTAQPSVQQIQLHESQQPTSQAQIV--------------- 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 102 qiiQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAVNPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGlSQQL 181
Cdd:cd22537   364 ---QGITQQAIQGVQALGAQAIPQQALQNLQLQLLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAP-AQQI 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 182 TITPVSSsggTTLAQI-APVAVAGAPITLNTAQLasvPNLQTVSVANLGAAGVQVQgvpvtitsvagqqQGQDGVKVQQA 260
Cdd:cd22537   440 TLTPVQT---LTLGQVgAGGAITSTPVSLSTGQL---PNLQTVTVNSIDSAGIQLQ-------------QSENADSPADI 500

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1030311313 261 TIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEpGKKKQHI 335
Cdd:cd22537   501 QIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNL-GKKKQHI 574
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 128-335 2.21e-25

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: 108.06  E-value: 2.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 128 LQNVQLQAV-NPTQVLIRAPtLTPSGQISWQTVQVQNIQSlsnlqvqnaglsqqltitpvsssggttlaqiapvavagap 206
Cdd:cd22539   284 LQNLQIQTVpNSGPIIIRTP-VGPNGQVSWQTIQLQNLQT---------------------------------------- 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 207 ITLNTAQLASVPNLQTVSVANLGAAGVQV---QGVPVTITSVAGQQQGQDGVKvqqatiapvtvAVGGIANATIGAVspd 283
Cdd:cd22539   323 VTVNAAQLSSMPGLQTINLNALGASGIQVhqlQGLPLTIANATGEHGAQLGLH-----------GAGGDGLHDDSAA--- 388

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1030311313 284 qltqvhlQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 335
Cdd:cd22539   389 -------EEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 127-335 2.83e-25

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 108.48  E-value: 2.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 127 PLQNVQLQAVNP--TQVLIRaptlTPSGQISWQTVQVQNI----QSLSNLQVQNAGLSQQLTITPVSSSG---GTTLAQI 197
Cdd:cd22540   325 PLQNIQIQNSEPtpTQVYIK----TPSGEVQTVLLQEAPAatatPSSSTSTVQQQVTANNGTGTSKPNYNvrkERTLPKI 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 198 APvavAGAPITLNTAQLASVPN-LQTVSVAnlgaaGVQVQGVPVTITSVAGQQQGqdgvkvqqatiapVTVAVGGiANAT 276
Cdd:cd22540   401 AP---AGGIISLNAAQLAAAAQaIQTININ-----GVQVQGVPVTITNAGGQQQL-------------TVQTVSS-NNLT 458

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1030311313 277 IGAVSPdqlTQVHLQQGQQTSDQeVQPGKRLRRVACSCPNCREGEGRgSNEPGKKKqHI 335
Cdd:cd22540   459 ISGLSP---TQIQLQMEQALEIE-TQPGEKRRRMACTCPNCKDGEKR-SGEQGKKK-HI 511
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 295-335 3.60e-16

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: 73.25  E-value: 3.60e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1030311313 295 QTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEpGKKKQHI 335
Cdd:cd22545    43 QFQDQEPQPGKRLRRVACTCPNCKDGEGRGSED-GKKKQHI 82
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 149-335 4.67e-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: 61.20  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 149 TPSGQISWQTVqVQNIQSLSNLQVQNAGLSQQLTITPVSSSGGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANL 228
Cdd:cd22553   216 QVSSQGYIQQI-PANASQQQPQMVQQGPNQSGQIIGQVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVTSPIQGM 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 229 gaagvqVQGVPVTITSVAGQQQGQdgvkvQQATIAPVTVAVGGIANATIGAVSPDQLTQvhlqqGQQTSDQEVQPGKRLR 308
Cdd:cd22553   295 ------TQGLTAPASSSIPTVVQQ-----QAIQGNPLPPGTQIIAAGQQLQQDPNDPTK-----WQVVADGTPGSKKRLR 358

                         170       180
                  ....*....|....*....|....*..
gi 1030311313 309 RVACSCPNCREGEGRGSNEpGKKKQHI 335
Cdd:cd22553   359 RVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-403 9.10e-09

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 9.10e-09
                          10        20
                  ....*....|....*....|....
gi 1030311313 380 ELQRHRRTHTGEKRFECPECSKRF 403
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 1.59e-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: 1.59e-05
                          10        20
                  ....*....|....*....|...
gi 1030311313 394 FECPECSKRFMRSDHLSKHVKTH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-420 2.04e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030311313 349 SHLRAHLRW--HTGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHVKTHQNKK 420
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 364-388 2.95e-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: 40.75  E-value: 2.95e-05
                          10        20
                  ....*....|....*....|....*
gi 1030311313 364 FICNwmFCGKRFTRSDELQRHRRTH 388
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 230-335 5.90e-05

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: 42.94  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311313 230 AAGVQVQGVPVTITSVAGQQQGQDGVK------VQQATIAPVTVAVGGIANATiGAVSPDQLTqvHLQQGQQTSDQEVQP 303
Cdd:cd22541    40 AASAPPHPSPVSSPTQQPQQLPPNPADdipwwsIQQSNPAHPPSTSTPLGHPT-FAGYQPQIA--ALLQTKSPAASLSTT 116

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1030311313 304 gKRLRRvaCSCPNCREGEGrgSNEPGKKKQHI 335
Cdd:cd22541   117 -RRCRR--CRCPNCQNPST--SSEPGKKKQHI 143
zf-H2C2_2 pfam13465
Zinc-finger double domain;
350-377 6.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 6.52e-05
                          10        20
                  ....*....|....*....|....*...
gi 1030311313 350 HLRAHLRWHTGERPFICnwMFCGKRFTR 377
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 394-416 1.02e-04

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 39.16  E-value: 1.02e-04
                          10        20
                  ....*....|....*....|...
gi 1030311313 394 FECPECSKRFMRSDHLSKHVKTH 416
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
ZnF_C2H2 smart00355
zinc finger;
394-416 4.21e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 4.21e-04
                           10        20
                   ....*....|....*....|...
gi 1030311313  394 FECPECSKRFMRSDHLSKHVKTH 416
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
364-388 2.08e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.08e-03
                           10        20
                   ....*....|....*....|....*
gi 1030311313  364 FICNWmfCGKRFTRSDELQRHRRTH 388
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 364-388 4.63e-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: 4.63e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311313 364 FICNwmFCGKRFTRSDELQRHRRTH 388
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 334-358 5.54e-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: 5.54e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311313 334 HICHIegCGKVYGKTSHLRAHLRWH 358
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
362-420 7.29e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 7.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1030311313 362 RPFICNwmFCGKRFTRSDELQRHRRTHTGEKRFEC--PECSKRFMRSDHLSKHVKTHQNKK 420
Cdd:COG5048    32 RPDSCP--NCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNP 90
 
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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