NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41056247|ref|NP_956418|]
View 

transcription factor Sp4 [Danio rerio]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 28-577 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: 591.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247  28 SGSQDAQPSPLALLAATCSKIGGVGAEGQAAAQQQIIIDPNQGLLQLQNPTQQLELVPAQLTGNGWQIIATSPATATKDS 107
Cdd:cd22536   7 SGSQDSQPSPLALLAATCSKIGTPGENQGAGQQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPPTSKENN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 108 IQQAGANAASSEAAAG---------RKVKAVGSNNAAQQQFQIIQVQNLPNSSGGIQYQVIPHLQTADGQQIQISPSNPA 178
Cdd:cd22536  87 VAQQGVSAATSSAAPSssnngstspTKVKAGNSNASAPGQFQVIQVQNMQNPSGSVQYQVIPQIQTVEGQQIQISPANAT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 179 ALSVQPEQIQLISTGNNQAILATPQRTGSASIV----QNQTIPLQIRP--SFPLQLQTIQGTQAPMVTTLPINLGGVTLA 252
Cdd:cd22536 167 ALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIaqnlANQTVPVQIRPgvSIPLQLQTIPGAQAQVVTTLPINIGGVTLA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 253 LPVINNVAGAGGSVQLLQSSDGSISNGNQLITTVTTSTA--------DSTGSSTSTTTATGSDSVVVTSADGLSTTSMVS 324
Cdd:cd22536 247 LPVINNVAAGGGSGQLVQPSDGGVSNGNQLVSTPITTASvstmpespSSSTTCTTTASTSLTSSDTLVSSAETGQYASTA 326

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 325 AESP-------------KDNEADLTQSNGLQSTSEQAGQIQ----------QFQIVGHPVLQQIQIQSPQQQVVQGSIQI 381
Cdd:cd22536 327 ASSErteeepqtsaaesEAQSSSQLQSNGLQNVQDQSNSLQqvqivgqpilQQIQIQQPQQQIIQAIQPQSFQLQSGQTI 406

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 382 QpgQTLQPVQQNLQLQAFQNPAQVLIRTPTLTPSGQISWQTVQVQN-----------AGMPQQLTLAPVASSAGGGTFAQ 450
Cdd:cd22536 407 Q--TIQQQPLQNVQLQAVQSPTQVLIRAPTLTPSGQISWQTVQVQNiqslsnlqvqnAGLPQQLTLTPVSSSAGGTTIAQ 484

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 451 IAPLTLGGSPITLSAAQLPAGSGVQTVNIAGLGAAGVQVQGVPLTITGVQGQQQGQDGVKVQS---APVTVTVGNISN-- 525
Cdd:cd22536 485 IAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQatiAPVTVAVGNIANat 564

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41056247 526 --AVSPEQMGQVQS-----PSDQEGQPSKRLRRVACSCPNCRDGEGRNNSDPSKKKQHV 577
Cdd:cd22536 565 igAVSPDQITQVQLqqaqqASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
622-645 1.36e-08

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.36e-08
                          10        20
                  ....*....|....*....|....
gi 41056247   622 ELQRHRRTHTGEKRFECPECSKRF 645
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-619 3.71e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 3.71e-06
                          10        20
                  ....*....|....*....|....*...
gi 41056247   592 HLRAHLRWHTGERPFVCnwIFCGKRFTR 619
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 636-658 6.95e-06

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 43.06  E-value: 6.95e-06
                          10        20
                  ....*....|....*....|...
gi 41056247   636 FECPECSKRFMRSDHLSKHIKTH 658
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 576-600 9.36e-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: 9.36e-03
                          10        20
                  ....*....|....*....|....*
gi 41056247   576 HVCHmeGCGKVYGKTSHLRAHLRWH 600
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 28-577 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: 591.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247  28 SGSQDAQPSPLALLAATCSKIGGVGAEGQAAAQQQIIIDPNQGLLQLQNPTQQLELVPAQLTGNGWQIIATSPATATKDS 107
Cdd:cd22536   7 SGSQDSQPSPLALLAATCSKIGTPGENQGAGQQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPPTSKENN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 108 IQQAGANAASSEAAAG---------RKVKAVGSNNAAQQQFQIIQVQNLPNSSGGIQYQVIPHLQTADGQQIQISPSNPA 178
Cdd:cd22536  87 VAQQGVSAATSSAAPSssnngstspTKVKAGNSNASAPGQFQVIQVQNMQNPSGSVQYQVIPQIQTVEGQQIQISPANAT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 179 ALSVQPEQIQLISTGNNQAILATPQRTGSASIV----QNQTIPLQIRP--SFPLQLQTIQGTQAPMVTTLPINLGGVTLA 252
Cdd:cd22536 167 ALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIaqnlANQTVPVQIRPgvSIPLQLQTIPGAQAQVVTTLPINIGGVTLA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 253 LPVINNVAGAGGSVQLLQSSDGSISNGNQLITTVTTSTA--------DSTGSSTSTTTATGSDSVVVTSADGLSTTSMVS 324
Cdd:cd22536 247 LPVINNVAAGGGSGQLVQPSDGGVSNGNQLVSTPITTASvstmpespSSSTTCTTTASTSLTSSDTLVSSAETGQYASTA 326

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 325 AESP-------------KDNEADLTQSNGLQSTSEQAGQIQ----------QFQIVGHPVLQQIQIQSPQQQVVQGSIQI 381
Cdd:cd22536 327 ASSErteeepqtsaaesEAQSSSQLQSNGLQNVQDQSNSLQqvqivgqpilQQIQIQQPQQQIIQAIQPQSFQLQSGQTI 406

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 382 QpgQTLQPVQQNLQLQAFQNPAQVLIRTPTLTPSGQISWQTVQVQN-----------AGMPQQLTLAPVASSAGGGTFAQ 450
Cdd:cd22536 407 Q--TIQQQPLQNVQLQAVQSPTQVLIRAPTLTPSGQISWQTVQVQNiqslsnlqvqnAGLPQQLTLTPVSSSAGGTTIAQ 484

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 451 IAPLTLGGSPITLSAAQLPAGSGVQTVNIAGLGAAGVQVQGVPLTITGVQGQQQGQDGVKVQS---APVTVTVGNISN-- 525
Cdd:cd22536 485 IAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQatiAPVTVAVGNIANat 564

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41056247 526 --AVSPEQMGQVQS-----PSDQEGQPSKRLRRVACSCPNCRDGEGRNNSDPSKKKQHV 577
Cdd:cd22536 565 igAVSPDQITQVQLqqaqqASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
622-645 1.36e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.36e-08
                          10        20
                  ....*....|....*....|....
gi 41056247   622 ELQRHRRTHTGEKRFECPECSKRF 645
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-619 3.71e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 3.71e-06
                          10        20
                  ....*....|....*....|....*...
gi 41056247   592 HLRAHLRWHTGERPFVCnwIFCGKRFTR 619
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 636-658 6.95e-06

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 43.06  E-value: 6.95e-06
                          10        20
                  ....*....|....*....|...
gi 41056247   636 FECPECSKRFMRSDHLSKHIKTH 658
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-656 4.59e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 4.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 566 NNSDPSKKKQHVCHMEGCGKVYGKTSHLRAHLRWHTGERPFVCNWIFCGKRFTRSDELQRHRRTHTgEKRFECPECSKRF 645
Cdd:COG5048 377 QYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSF 455

                        90
                ....*....|.
gi 41056247 646 MRSDHLSKHIK 656
Cdd:COG5048 456 RRDLDLSNHGK 466
ZnF_C2H2 smart00355
zinc finger;
636-658 2.61e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.60  E-value: 2.61e-04
                           10        20
                   ....*....|....*....|...
gi 41056247    636 FECPECSKRFMRSDHLSKHIKTH 658
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
606-630 1.17e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.17e-03
                           10        20
                   ....*....|....*....|....*
gi 41056247    606 FVCNWifCGKRFTRSDELQRHRRTH 630
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 ...
 576-600 9.36e-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: 9.36e-03
                          10        20
                  ....*....|....*....|....*
gi 41056247   576 HVCHmeGCGKVYGKTSHLRAHLRWH 600
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 28-577 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: 591.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247  28 SGSQDAQPSPLALLAATCSKIGGVGAEGQAAAQQQIIIDPNQGLLQLQNPTQQLELVPAQLTGNGWQIIATSPATATKDS 107
Cdd:cd22536   7 SGSQDSQPSPLALLAATCSKIGTPGENQGAGQQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPPTSKENN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 108 IQQAGANAASSEAAAG---------RKVKAVGSNNAAQQQFQIIQVQNLPNSSGGIQYQVIPHLQTADGQQIQISPSNPA 178
Cdd:cd22536  87 VAQQGVSAATSSAAPSssnngstspTKVKAGNSNASAPGQFQVIQVQNMQNPSGSVQYQVIPQIQTVEGQQIQISPANAT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 179 ALSVQPEQIQLISTGNNQAILATPQRTGSASIV----QNQTIPLQIRP--SFPLQLQTIQGTQAPMVTTLPINLGGVTLA 252
Cdd:cd22536 167 ALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIaqnlANQTVPVQIRPgvSIPLQLQTIPGAQAQVVTTLPINIGGVTLA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 253 LPVINNVAGAGGSVQLLQSSDGSISNGNQLITTVTTSTA--------DSTGSSTSTTTATGSDSVVVTSADGLSTTSMVS 324
Cdd:cd22536 247 LPVINNVAAGGGSGQLVQPSDGGVSNGNQLVSTPITTASvstmpespSSSTTCTTTASTSLTSSDTLVSSAETGQYASTA 326

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 325 AESP-------------KDNEADLTQSNGLQSTSEQAGQIQ----------QFQIVGHPVLQQIQIQSPQQQVVQGSIQI 381
Cdd:cd22536 327 ASSErteeepqtsaaesEAQSSSQLQSNGLQNVQDQSNSLQqvqivgqpilQQIQIQQPQQQIIQAIQPQSFQLQSGQTI 406

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 382 QpgQTLQPVQQNLQLQAFQNPAQVLIRTPTLTPSGQISWQTVQVQN-----------AGMPQQLTLAPVASSAGGGTFAQ 450
Cdd:cd22536 407 Q--TIQQQPLQNVQLQAVQSPTQVLIRAPTLTPSGQISWQTVQVQNiqslsnlqvqnAGLPQQLTLTPVSSSAGGTTIAQ 484

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 451 IAPLTLGGSPITLSAAQLPAGSGVQTVNIAGLGAAGVQVQGVPLTITGVQGQQQGQDGVKVQS---APVTVTVGNISN-- 525
Cdd:cd22536 485 IAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQatiAPVTVAVGNIANat 564

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41056247 526 --AVSPEQMGQVQS-----PSDQEGQPSKRLRRVACSCPNCRDGEGRNNSDPSKKKQHV 577
Cdd:cd22536 565 igAVSPDQITQVQLqqaqqASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 28-577 3.84e-44

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: 167.43  E-value: 3.84e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247  28 SGSQDAQPSPLALLAATCSKIGGVGAEgqaaaqqqiiiDPNQGLLQLQNPTQQLELVPAQLTG--NGWQIIATSPATATK 105
Cdd:cd22537   2 AAEQDTQPSPLALLAATCSKIGSPSPG-----------DDAAAAGNAASAGQTGDLASAQLTGapNRWEVLTPTPTTIKD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 106 DSIQQAGANAASSEAAAGRKVKAVGSNNAAQQQFQIIQVQNLPNSSGGIQYQVIPHLQTADGQQIQIS---PSNPAALSV 182
Cdd:cd22537  71 EAGNLVQIPGGGTVTSSGQYVLPLQSLQNQQIFSVAPGSDASNGTVPNVQYQVIPQIQTTDGQQVQLGfatSSDNTGLQQ 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 183 QPEQIQLIStGNNQAILATPQRTGSASIVQNQTIPLQIR------PSFPlqlqtiqgTQAPMVTTLPINLGGVTLALPvI 256
Cdd:cd22537 151 EGGQIQIIP-GSNQTIIASGTPSAVQQLLSQSGHVVQIQgvsiggSSFP--------GQTQVVANVPLGLPGNITFVP-I 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 257 NNV----AGAGGSVQLLQSS---DGSISNGNQLITTVTTSTADSTGSSTSTTTATGSDSVVVTSADGLSTTSMVSAESPK 329
Cdd:cd22537 221 NSVdldsLGLSGTSQTMTTGitaDGQLINTGQAVQSSDNSGESGKVSPDINETNTNADLFVPTSSSSQLPVTIDSTGILQ 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 330 DNEADLTQSNGLQSTSEQAGQIQQFQIVGHPVLQQIQIQSPQQQVVQGSIQIQPGQTLQP-------------------- 389
Cdd:cd22537 301 QNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHESQQPTSQAqivqgitqqaiqgvqalgaq 380

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 390 -----VQQNLQLQaFQNPAQVLIRTPTLTPSGQISWQTVQVQNAGMPQQLTLApvASSAGGGTFAQIAPLTLG------- 457
Cdd:cd22537 381 aipqqALQNLQLQ-LLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQ--NAPAQQITLTPVQTLTLGqvgagga 457

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 458 --GSPITLSAAQLPagsGVQTVNIAGLGAAGVQVQGVPLTiTGVQGQQQGQDGVKVQSAPVTVTVGNISNAVSPEQMGQV 535
Cdd:cd22537 458 itSTPVSLSTGQLP---NLQTVTVNSIDSAGIQLQQSENA-DSPADIQIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLV 533

                       570       580       590       600
                ....*....|....*....|....*....|....*....|..
gi 41056247 536 QSPSDQEGQPSKRLRRVACSCPNCRDGEGRnNSDPSKKKQHV 577
Cdd:cd22537 534 EEEGDQPHQEGKRLRRVACTCPNCKEGGGR-GSNLGKKKQHI 574
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 28-577 1.65e-43

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: 162.76  E-value: 1.65e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247  28 SGSQDAQPSPLALLAATCSKIGGVGAegqaaaqqqiiIDPNQGLLQLQNPTQQLELVPAQLT--GNGWQIIATSpATATK 105
Cdd:cd22539   2 SGGQESQPSPLALLAATCSRIESPNE-----------NSNSSQQQQQQQGELELDLTQAQIAqsANGWQIIPTG-SQAPT 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 106 DSIQQAGANAASSEAAAGRKVKAVGSNNAAQQQFQIIQVQNLPNSSGGIQYQVIPHLQTADGQQIQISPSNPAALSVQPE 185
Cdd:cd22539  70 PSKEQSGDSSTADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 186 QIQLISTGNNQAIlaTPQRTGSASIVqnqTIPLQIRPSFPLQ----LQTIQGTQAPMVTTLPINLGGVTLALPVinnvag 261
Cdd:cd22539 150 QLQIIPGTNQQII--TTNRSGSGNII---TMPNLLQQAVPIQglglANNVLPGQTQFVANVPVALNGNITLLPV------ 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 262 aggsvqllqsSDGSISNgnqlittvttstadstgsststttatgsdsvvVTSADGLSTTSmvsaespkdneadltqsngl 341
Cdd:cd22539 219 ----------SSVTASF--------------------------------FTNANSYSTTT-------------------- 236

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 342 qsTSEQAGQIQQfQIVGHPVLQQIQIQSPQQQVVQGSIQIQPGQTL-QPVQQNLQLQAFQNPAQVLIRTPtLTPSGQISW 420
Cdd:cd22539 237 --TTSNMGQQQQ-QILIQPQLVQGGQTIQALQAASLPGQTFTTQTIsQEALQNLQIQTVPNSGPIIIRTP-VGPNGQVSW 312

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 421 QTVQVQNAGMPqqltlapvassagggtfaqiapltlggspiTLSAAQLPAGSGVQTVNIAGLGAAGVQV---QGVPLTIT 497
Cdd:cd22539 313 QTIQLQNLQTV------------------------------TVNAAQLSSMPGLQTINLNALGASGIQVhqlQGLPLTIA 362

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 498 GVQGQQQGQDGVKVQSApvtvtvGNISNAVSPEQMGqvqSPSDQEGQPSKRLRRVACSCPNCRDGEGRNNSDPSKKKQHV 577
Cdd:cd22539 363 NATGEHGAQLGLHGAGG------DGLHDDSAAEEGE---TEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 28-574 3.91e-27

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: 116.18  E-value: 3.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247  28 SGSQDAQPSPLALLAATCSKIGGVGAEGQAAAQQQIIIDPNQGLLQLQNPtqqlelvpaQLTGNGWQIIATSPATATKDS 107
Cdd:cd22540  17 STTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAP---------LPLGPGKNSIGFLSAKGNIIQ 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 108 IQQAGANAASSEAAAGRKVKAVGSNNAAQQQfqiiqvqnlpNSSGGIQYQVIPHLQTADgqqiQISPSNpaalsvqpeQI 187
Cdd:cd22540  88 LQGSQLSSSAPGGQQVFAIQNPTMIIKGSQT----------RSSTNQQYQISPQIQAAG----QINNSG---------QI 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 188 QLIStGNNQAILATPQRTGSASIVQnQTIPLQIRPSFPLQLQTIQGTQAPMVTTLPINlGGVTLALPVINNVAGAGGSVQ 267
Cdd:cd22540 145 QIIP-GTNQAIITPVQVLQQPQQAH-KPVPIKPAPLQTSNTNSASLQVPGNVIKLQSG-GNVALTLPVNNLVGTQDGATQ 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 268 LLQSSDGSISNgnqlitTVTTSTADSTGSSTSTTTATGSDSVVVTSAD--GLSTTSMVSAESPKDNEADLTQSnglQSTS 345
Cdd:cd22540 222 LQLAAAPSKPS------KKIRKKSAQAAQPAVTVAEQVETVLIETTADniIQAGNNLLIVQSPGTGQPAVLQQ---VQVL 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 346 EQAGQIQQFQIVGHPVlqqiqiqSPQQQVVQGSIQIQpgqtlQPVQQNLQLQAFQ-NPAQVLIRTPtltpSGQISWQTVQ 424
Cdd:cd22540 293 QPKQEQQVVQIPQQAL-------RVVQAASATLPTVP-----QKPLQNIQIQNSEpTPTQVYIKTP----SGEVQTVLLQ 356

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 425 VQNAGMPQQLTLAPVASSAGGGTFAQIAPLTL--------------GGSPITLSAAQLP-AGSGVQTVNIAGlgaagVQV 489
Cdd:cd22540 357 EAPAATATPSSSTSTVQQQVTANNGTGTSKPNynvrkertlpkiapAGGIISLNAAQLAaAAQAIQTINING-----VQV 431

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 490 QGVPLTITGVQGqqqgqdgvkvQSAPVTVTVGNISNAVSPEQMGQVQSPSDQ----EGQPSKRLRRVACSCPNCRDGEGR 565
Cdd:cd22540 432 QGVPVTITNAGG----------QQQLTVQTVSSNNLTISGLSPTQIQLQMEQaleiETQPGEKRRRMACTCPNCKDGEKR 501


                ....*....
gi 41056247 566 nNSDPSKKK 574
Cdd:cd22540 502 -SGEQGKKK 509
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 528-577 8.76e-14

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


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 67.08  E-value: 8.76e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41056247 528 SPEQMGQVQ-----SPSDQEGQPSKRLRRVACSCPNCRDGEGRnNSDPSKKKQHV 577
Cdd:cd22545  29 STGPGGNIQyqvipQFQDQEPQPGKRLRRVACTCPNCKDGEGR-GSEDGKKKQHI 82
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 377-577 1.49e-09

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: 60.42  E-value: 1.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 377 GSIQIQPGQTLQPVQQNLQLQafqnPAQVLirtptlTPSGQISWQTV-QVQNAGMPQQLTLAPVASSAGGGTFAQIAPLT 455
Cdd:cd22553 190 GGNQALQAQVIPQLAQAAQLQ----PQQLA------QVSSQGYIQQIpANASQQQPQMVQQGPNQSGQIIGQVASASSIQ 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 456 LGGSPITLSAAqlpaGSGVQTVNIAGLGAAGVQVQGVPLTITGVQGQQQGQDGVKVQSAPVTVTVGNISNAVSPEQMGQv 535
Cdd:cd22553 260 AAAIPLTVYTG----ALAGQNGSNQQQVGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQGNPLPPGTQIIAAGQQLQ- 334

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 41056247 536 QSPSD-------QEGQP--SKRLRRVACSCPNCRDGEGRNNSDpSKKKQHV 577
Cdd:cd22553 335 QDPNDptkwqvvADGTPgsKKRLRRVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-H2C2_2 pfam13465
Zinc-finger double domain;
622-645 1.36e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.36e-08
                          10        20
                  ....*....|....*....|....
gi 41056247   622 ELQRHRRTHTGEKRFECPECSKRF 645
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 28-49 1.29e-07

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: 49.36  E-value: 1.29e-07
                        10        20
                ....*....|....*....|..
gi 41056247  28 SGSQDAQPSPLALLAATCSKIG 49
Cdd:cd22545   2 SSAQDSQPSPLALLAATCSKIG 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-619 3.71e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 3.71e-06
                          10        20
                  ....*....|....*....|....*...
gi 41056247   592 HLRAHLRWHTGERPFVCnwIFCGKRFTR 619
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 636-658 6.95e-06

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 43.06  E-value: 6.95e-06
                          10        20
                  ....*....|....*....|...
gi 41056247   636 FECPECSKRFMRSDHLSKHIKTH 658
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 606-630 2.68e-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: 2.68e-05
                          10        20
                  ....*....|....*....|....*
gi 41056247   606 FVCNwiFCGKRFTRSDELQRHRRTH 630
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-656 4.59e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 4.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056247 566 NNSDPSKKKQHVCHMEGCGKVYGKTSHLRAHLRWHTGERPFVCNWIFCGKRFTRSDELQRHRRTHTgEKRFECPECSKRF 645
Cdd:COG5048 377 QYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSF 455

                        90
                ....*....|.
gi 41056247 646 MRSDHLSKHIK 656
Cdd:COG5048 456 RRDLDLSNHGK 466
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 636-658 1.43e-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: 1.43e-04
                          10        20
                  ....*....|....*....|...
gi 41056247   636 FECPECSKRFMRSDHLSKHIKTH 658
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
ZnF_C2H2 smart00355
zinc finger;
636-658 2.61e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.60  E-value: 2.61e-04
                           10        20
                   ....*....|....*....|...
gi 41056247    636 FECPECSKRFMRSDHLSKHIKTH 658
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
591-662 3.29e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 3.29e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41056247 591 SHLRAHLRW--HTGE--RPFVCNWIFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHIKTHQNKK 662
Cdd:COG5048 303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 512-577 7.50e-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: 40.62  E-value: 7.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41056247 512 QSAPVTVTV---GNISNAVSPEQMGQV-QSPSDQEGQP-SKRLRRvaCSCPNCRDGEgrNNSDPSKKKQHV 577
Cdd:cd22541  77 NPAHPPSTStplGHPTFAGYQPQIAALlQTKSPAASLStTRRCRR--CRCPNCQNPS--TSSEPGKKKQHI 143
ZnF_C2H2 smart00355
zinc finger;
606-630 1.17e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 1.17e-03
                           10        20
                   ....*....|....*....|....*
gi 41056247    606 FVCNWifCGKRFTRSDELQRHRRTH 630
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.
 606-630 7.83e-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: 7.83e-03
                          10        20
                  ....*....|....*....|....*
gi 41056247   606 FVCNwiFCGKRFTRSDELQRHRRTH 630
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 ...
 576-600 9.36e-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: 9.36e-03
                          10        20
                  ....*....|....*....|....*
gi 41056247   576 HVCHmeGCGKVYGKTSHLRAHLRWH 600
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH