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Conserved domains on  [gi|67010025|ref|NP_003103|]
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transcription factor Sp4 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 32-648 0e+00

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: 741.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025  32 NKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQ-QQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPP 110
Cdd:cd22536   1 NKKGKTSGSQDSQPSPLALLAATCSKIGTPGENQGAGQqQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 111 ASKENNVSQP----ASSSSSSSSSNNGSASPTKTKSGNS--STPGQFQVIQVQ---NPSGSVQYQVIPQLQTVEGQQIQI 181
Cdd:cd22536  81 TSKENNVAQQgvsaATSSAAPSSSNNGSTSPTKVKAGNSnaSAPGQFQVIQVQnmqNPSGSVQYQVIPQIQTVEGQQIQI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 182 NPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINI 261
Cdd:cd22536 161 SPANATALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIAQNLANQTVPVQIRPGVSIPLQLQTIPGAQAQVVTTLPINI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 262 GGVTLALPVINNVAAGGGTGQVGQPAataDSGTSNGNQLVSTPTnTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSS 341
Cdd:cd22536 241 GGVTLALPVINNVAAGGGSGQLVQPS---DGGVSNGNQLVSTPI-TTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSS 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 342 ADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIP 421
Cdd:cd22536 317 AETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQ 394

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 422 PQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVS 500
Cdd:cd22536 395 PQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLPQQLTLTPVS 474

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 501 SS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 579
Cdd:cd22536 475 SSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 554

                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67010025 580 VAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 648
Cdd:cd22536 555 VAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
693-716 1.49e-08

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.49e-08
                          10        20
                  ....*....|....*....|....
gi 67010025   693 ELQRHRRTHTGEKRFECPECSKRF 716
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 707-729 2.61e-05

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.52  E-value: 2.61e-05
                          10        20
                  ....*....|....*....|...
gi 67010025   707 FECPECSKRFMRSDHLSKHVKTH 729
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 677-701 4.85e-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: 4.85e-05
                          10        20
                  ....*....|....*....|....*
gi 67010025   677 FICNwmFCGKRFTRSDELQRHRRTH 701
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 ...
 647-671 9.12e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 9.12e-03
                          10        20
                  ....*....|....*....|....*
gi 67010025   647 HICHIegCGKVYGKTSHLRAHLRWH 671
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 ...
 32-648 0e+00

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: 741.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025  32 NKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQ-QQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPP 110
Cdd:cd22536   1 NKKGKTSGSQDSQPSPLALLAATCSKIGTPGENQGAGQqQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 111 ASKENNVSQP----ASSSSSSSSSNNGSASPTKTKSGNS--STPGQFQVIQVQ---NPSGSVQYQVIPQLQTVEGQQIQI 181
Cdd:cd22536  81 TSKENNVAQQgvsaATSSAAPSSSNNGSTSPTKVKAGNSnaSAPGQFQVIQVQnmqNPSGSVQYQVIPQIQTVEGQQIQI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 182 NPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINI 261
Cdd:cd22536 161 SPANATALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIAQNLANQTVPVQIRPGVSIPLQLQTIPGAQAQVVTTLPINI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 262 GGVTLALPVINNVAAGGGTGQVGQPAataDSGTSNGNQLVSTPTnTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSS 341
Cdd:cd22536 241 GGVTLALPVINNVAAGGGSGQLVQPS---DGGVSNGNQLVSTPI-TTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSS 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 342 ADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIP 421
Cdd:cd22536 317 AETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQ 394

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 422 PQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVS 500
Cdd:cd22536 395 PQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLPQQLTLTPVS 474

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 501 SS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 579
Cdd:cd22536 475 SSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 554

                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67010025 580 VAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 648
Cdd:cd22536 555 VAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
693-716 1.49e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.49e-08
                          10        20
                  ....*....|....*....|....
gi 67010025   693 ELQRHRRTHTGEKRFECPECSKRF 716
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 707-729 2.61e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.52  E-value: 2.61e-05
                          10        20
                  ....*....|....*....|...
gi 67010025   707 FECPECSKRFMRSDHLSKHVKTH 729
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 677-701 4.85e-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: 4.85e-05
                          10        20
                  ....*....|....*....|....*
gi 67010025   677 FICNwmFCGKRFTRSDELQRHRRTH 701
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
663-690 1.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.07e-04
                          10        20
                  ....*....|....*....|....*...
gi 67010025   663 HLRAHLRWHTGERPFICnwMFCGKRFTR 690
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
662-733 3.74e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 3.74e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67010025 662 SHLRAHLRW--HTGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHVKTHQNKK 733
Cdd:COG5048 303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
707-729 4.00e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 4.00e-04
                           10        20
                   ....*....|....*....|...
gi 67010025    707 FECPECSKRFMRSDHLSKHVKTH 729
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
677-701 2.00e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|....*
gi 67010025    677 FICNWmfCGKRFTRSDELQRHRRTH 701
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 ...
 647-671 9.12e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 9.12e-03
                          10        20
                  ....*....|....*....|....*
gi 67010025   647 HICHIegCGKVYGKTSHLRAHLRWH 671
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 ...
 32-648 0e+00

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: 741.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025  32 NKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQ-QQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPP 110
Cdd:cd22536   1 NKKGKTSGSQDSQPSPLALLAATCSKIGTPGENQGAGQqQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 111 ASKENNVSQP----ASSSSSSSSSNNGSASPTKTKSGNS--STPGQFQVIQVQ---NPSGSVQYQVIPQLQTVEGQQIQI 181
Cdd:cd22536  81 TSKENNVAQQgvsaATSSAAPSSSNNGSTSPTKVKAGNSnaSAPGQFQVIQVQnmqNPSGSVQYQVIPQIQTVEGQQIQI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 182 NPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINI 261
Cdd:cd22536 161 SPANATALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIAQNLANQTVPVQIRPGVSIPLQLQTIPGAQAQVVTTLPINI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 262 GGVTLALPVINNVAAGGGTGQVGQPAataDSGTSNGNQLVSTPTnTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSS 341
Cdd:cd22536 241 GGVTLALPVINNVAAGGGSGQLVQPS---DGGVSNGNQLVSTPI-TTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSS 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 342 ADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIP 421
Cdd:cd22536 317 AETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQ 394

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 422 PQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVS 500
Cdd:cd22536 395 PQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLPQQLTLTPVS 474

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 501 SS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 579
Cdd:cd22536 475 SSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 554

                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67010025 580 VAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 648
Cdd:cd22536 555 VAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 37-648 1.70e-58

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: 209.03  E-value: 1.70e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025  37 TSGSQDSQPSPLALLAATCSKIGTPGENqatgqqqiiiDPSQGLVQLQNQPQQLELVTTQLAG--NAWQLVASTPPASKE 114
Cdd:cd22537   1 GAAEQDTQPSPLALLAATCSKIGSPSPG----------DDAAAAGNAASAGQTGDLASAQLTGapNRWEVLTPTPTTIKD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 115 NNVSQPASSSSSSSSSNNGSASPTKTKSGNSstpgQFQVIQVQNPSG----SVQYQVIPQLQTVEGQQIQINPTSSS--- 187
Cdd:cd22537  71 EAGNLVQIPGGGTVTSSGQYVLPLQSLQNQQ----IFSVAPGSDASNgtvpNVQYQVIPQIQTTDGQQVQLGFATSSdnt 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 188 SLQDLQGQIQLISaGNNQAILTAANRTASgnilAQNLANQTVPVQIrPGVSIPlqlQTLPGTQAQVVTTLPINIGGVTLA 267
Cdd:cd22537 147 GLQQEGGQIQIIP-GSNQTIIASGTPSAV----QQLLSQSGHVVQI-QGVSIG---GSSFPGQTQVVANVPLGLPGNITF 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 268 LPvINNVAAG----GGTGQVGQPAATADSGTSNGNQLVSTPTNTTTSASTMPESPSSST--------TCTTTASTSLTSS 335
Cdd:cd22537 218 VP-INSVDLDslglSGTSQTMTTGITADGQLINTGQAVQSSDNSGESGKVSPDINETNTnadlfvptSSSSQLPVTIDST 296

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 336 DTLVSSADTGQYASTSASSSERTIEESQTPAATESEAQS---SSQLQPNGMQNAQDQSNSLQQVQIVgqpilqqiqiqqp 412
Cdd:cd22537 297 GILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNiqvSTAQPSVQQIQLHESQQPTSQAQIV------------- 363

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 413 qqqiiQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAVNPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGlSQ 492
Cdd:cd22537 364 -----QGITQQAIQGVQALGAQAIPQQALQNLQLQLLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAP-AQ 437

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 493 QLTITPVSSsggTTLAQI-APVAVAGAPITLNTAQLasvPNLQTVSVANLGAAGVQVQgvpvtitsvagqqQGQDGVKVQ 571
Cdd:cd22537 438 QITLTPVQT---LTLGQVgAGGAITSTPVSLSTGQL---PNLQTVTVNSIDSAGIQLQ-------------QSENADSPA 498

                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67010025 572 QATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEpGKKKQHI 648
Cdd:cd22537 499 DIQIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNL-GKKKQHI 574
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 38-648 1.38e-44

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: 166.23  E-value: 1.38e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025  38 SGSQDSQPSPLALLAATCSKIGTPGENQATGQQQiiidpsqglvQLQNQPQQLELVTTQLA--GNAWQLVASTPPASKEN 115
Cdd:cd22539   2 SGGQESQPSPLALLAATCSRIESPNENSNSSQQQ----------QQQQGELELDLTQAQIAqsANGWQIIPTGSQAPTPS 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 116 NvSQPASSSSSSSSSNNGSASPTKTKSGNSSTPGQFQVIQVQNPSGSVQYQVIPQLQTVEGQQIQINPTSSSSLQDLQGQ 195
Cdd:cd22539  72 K-EQSGDSSTADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQ 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 196 IQLISAGNNQAIltAANRTASGNILAQ-NLANQTVPVQirpgvSIPLQLQTLPGtQAQVVTTLPINIGGVTLALPViNNV 274
Cdd:cd22539 151 LQIIPGTNQQII--TTNRSGSGNIITMpNLLQQAVPIQ-----GLGLANNVLPG-QTQFVANVPVALNGNITLLPV-SSV 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 275 AAgggtgqvgqpaatadSGTSNGNQLVSTptnTTTSAstmpespsssttctttastsltssdtlvssadtgqyastsass 354
Cdd:cd22539 222 TA---------------SFFTNANSYSTT---TTTSN------------------------------------------- 240

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 355 sertieesqtpaateSEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGqpilqqiqiqqpqqqiiqaippQSFQLQSgqtiq 434
Cdd:cd22539 241 ---------------MGQQQQQILIQPQLVQGGQTIQALQAASLPG----------------------QTFTTQT----- 278

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 435 tIQQQPLQNVQLQAV-NPTQVLIRAPtLTPSGQISWQTVQVQNIQSlsnlqvqnaglsqqltitpvsssggttlaqiapv 513
Cdd:cd22539 279 -ISQEALQNLQIQTVpNSGPIIIRTP-VGPNGQVSWQTIQLQNLQT---------------------------------- 322

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 514 avagapITLNTAQLASVPNLQTVSVANLGAAGVQV---QGVPVTITSVAGQQQGQDGVKvqqatiapvtvAVGGIANATI 590
Cdd:cd22539 323 ------VTVNAAQLSSMPGLQTINLNALGASGIQVhqlQGLPLTIANATGEHGAQLGLH-----------GAGGDGLHDD 385

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67010025 591 GAVspdqltqvhlQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 648
Cdd:cd22539 386 SAA----------EEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 34-645 4.83e-29

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: 121.96  E-value: 4.83e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025  34 KPKTSGSQDSQPSPLALLAATCSKIGTPGenqatgqQQIIIDPSQGLvqlqnQPQQLELVTtqlagnawQLVASTPPASK 113
Cdd:cd22540  13 QPAASTTQDSQPSPLALLAATCSKIGPPA-------VEAAVTPPAPP-----QPTPRKLVP--------IKPAPLPLGPG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 114 ENNVSQPASSSSSSSSSNNGsasptktksGNSSTPGQFQVIQVQNP-----------SGSVQYQVIPQLQTvegqqiqin 182
Cdd:cd22540  73 KNSIGFLSAKGNIIQLQGSQ---------LSSSAPGGQQVFAIQNPtmiikgsqtrsSTNQQYQISPQIQA--------- 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 183 ptssSSLQDLQGQIQLISaGNNQAILTAANRTASGNILAQnlanqtvPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINiG 262
Cdd:cd22540 135 ----AGQINNSGQIQIIP-GTNQAIITPVQVLQQPQQAHK-------PVPIKPAPLQTSNTNSASLQVPGNVIKLQSG-G 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 263 GVTLALPVINNVAAGGGTGQVGQPAATADSGTSNGNQlvstptntttsastmpespsssttctttastsltssdtlvsSA 342
Cdd:cd22540 202 NVALTLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKK-----------------------------------------SA 240

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 343 DTGQYASTSASSSERTIEESQTPAATESEAQSSSQLQPNGMQNAQdqsnsLQQVQIVgqpilqqIQIQQPQQQIIQAIPP 422
Cdd:cd22540 241 QAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAV-----LQQVQVL-------QPKQEQQVVQIPQQAL 308

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 423 QSFQLQSgQTIQTIQQQPLQNVQLQAVN--PTQVLIRaptlTPSGQISWQTVQVQNI----QSLSNLQVQNAGLSQQLTI 496
Cdd:cd22540 309 RVVQAAS-ATLPTVPQKPLQNIQIQNSEptPTQVYIK----TPSGEVQTVLLQEAPAatatPSSSTSTVQQQVTANNGTG 383

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 497 TPVSSSG---GTTLAQIAPvavAGAPITLNTAQLASVPN-LQTVSVanlgaAGVQVQGVPVTITSVAGQQQGqdgvkvqq 572
Cdd:cd22540 384 TSKPNYNvrkERTLPKIAP---AGGIISLNAAQLAAAAQaIQTINI-----NGVQVQGVPVTITNAGGQQQL-------- 447

                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67010025 573 atiapVTVAVGGiANATIGAVSPDQLTqvhlQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRgSNEPGKKK 645
Cdd:cd22540 448 -----TVQTVSS-NNLTISGLSPTQIQ----LQMEQALEIETQPGEKRRRMACTCPNCKDGEKR-SGEQGKKK 509
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 608-648 4.66e-15

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


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 70.94  E-value: 4.66e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 67010025 608 QTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEpGKKKQHI 648
Cdd:cd22545  43 QFQDQEPQPGKRLRRVACTCPNCKDGEGRGSED-GKKKQHI 82
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 37-72 5.98e-11

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: 58.99  E-value: 5.98e-11
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 67010025  37 TSGSQDSQPSPLALLAATCSKIGTPGENQATGQQQI 72
Cdd:cd22545   1 TSSAQDSQPSPLALLAATCSKIGSPAENSTGPGGNI 36
zf-H2C2_2 pfam13465
Zinc-finger double domain;
693-716 1.49e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.49e-08
                          10        20
                  ....*....|....*....|....
gi 67010025   693 ELQRHRRTHTGEKRFECPECSKRF 716
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 462-648 4.56e-07

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 52.72  E-value: 4.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 462 TPSGQISWQTVqVQNIQSLSNLQVQNAGLSQQLTITPVSSSGGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANL 541
Cdd:cd22553 216 QVSSQGYIQQI-PANASQQQPQMVQQGPNQSGQIIGQVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVTSPIQGM 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 542 gaagvqVQGVPVTITSVAGQQQGQdgvkvQQATIAPVTVAVGGIANATIGAVSPDQLTQvhlqqGQQTSDQEVQPGKRLR 621
Cdd:cd22553 295 ------TQGLTAPASSSIPTVVQQ-----QAIQGNPLPPGTQIIAAGQQLQQDPNDPTK-----WQVVADGTPGSKKRLR 358

                       170       180
                ....*....|....*....|....*..
gi 67010025 622 RVACSCPNCREGEGRGSNEpGKKKQHI 648
Cdd:cd22553 359 RVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 707-729 2.61e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.52  E-value: 2.61e-05
                          10        20
                  ....*....|....*....|...
gi 67010025   707 FECPECSKRFMRSDHLSKHVKTH 729
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 677-701 4.85e-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: 4.85e-05
                          10        20
                  ....*....|....*....|....*
gi 67010025   677 FICNwmFCGKRFTRSDELQRHRRTH 701
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
663-690 1.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.07e-04
                          10        20
                  ....*....|....*....|....*...
gi 67010025   663 HLRAHLRWHTGERPFICnwMFCGKRFTR 690
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.
 707-729 1.68e-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: 1.68e-04
                          10        20
                  ....*....|....*....|...
gi 67010025   707 FECPECSKRFMRSDHLSKHVKTH 729
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
662-733 3.74e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 3.74e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67010025 662 SHLRAHLRW--HTGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHVKTHQNKK 733
Cdd:COG5048 303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
707-729 4.00e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 4.00e-04
                           10        20
                   ....*....|....*....|...
gi 67010025    707 FECPECSKRFMRSDHLSKHVKTH 729
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 543-648 4.11e-04

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: 41.40  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67010025 543 AAGVQVQGVPVTITSVAGQQQGQDGVK------VQQATIAPVTVAVGGIANATiGAVSPDQLTqvHLQQGQQTSDQEVQP 616
Cdd:cd22541  40 AASAPPHPSPVSSPTQQPQQLPPNPADdipwwsIQQSNPAHPPSTSTPLGHPT-FAGYQPQIA--ALLQTKSPAASLSTT 116

                        90       100       110
                ....*....|....*....|....*....|..
gi 67010025 617 gKRLRRvaCSCPNCREGEGrgSNEPGKKKQHI 648
Cdd:cd22541 117 -RRCRR--CRCPNCQNPST--SSEPGKKKQHI 143
ZnF_C2H2 smart00355
zinc finger;
677-701 2.00e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|....*
gi 67010025    677 FICNWmfCGKRFTRSDELQRHRRTH 701
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.
 677-701 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|....*
gi 67010025   677 FICNwmFCGKRFTRSDELQRHRRTH 701
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 ...
 647-671 9.12e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 9.12e-03
                          10        20
                  ....*....|....*....|....*
gi 67010025   647 HICHIegCGKVYGKTSHLRAHLRWH 671
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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