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Conserved domains on  [gi|578831275|ref|XP_006722086|]
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transcription factor Sp2 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 9-526 0e+00

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: 613.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275   9 AATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILS 88
Cdd:cd22540    1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  89 SKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKG--TRSNANIQYQAVPQIQASNsqtiqvQPNLTNQIQIIPGTNQAI 166
Cdd:cd22540   81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGsqTRSSTNQQYQISPQIQAAG------QINNSGQIQIIPGTNQAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 167 ITP------SPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGgNVTLTLPVNNLVNASDTGAPTQLltespPTPL 240
Cdd:cd22540  155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 241 SKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 320
Cdd:cd22540  229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 321 LRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASraPHLSGTSKK 400
Cdd:cd22540  308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQV--TANNGTGTS 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 401 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 480
Cdd:cd22540  386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 578831275 481 QIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 526
Cdd:cd22540  466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
571-594 8.73e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 8.73e-07
                          10        20
                  ....*....|....*....|....
gi 578831275  571 ELQRHARTHTGDKRFECAQCQKRF 594
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
542-568 1.97e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.97e-05
                          10        20
                  ....*....|....*....|....*..
gi 578831275  542 LRAHVRLHTGERPFVCNwfFCGKRFTR 568
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 585-607 5.95e-05

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 40.36  E-value: 5.95e-05
                          10        20
                  ....*....|....*....|...
gi 578831275  585 FECAQCQKRFMRSDHLTKHYKTH 607
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 9-526 0e+00

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: 613.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275   9 AATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILS 88
Cdd:cd22540    1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  89 SKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKG--TRSNANIQYQAVPQIQASNsqtiqvQPNLTNQIQIIPGTNQAI 166
Cdd:cd22540   81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGsqTRSSTNQQYQISPQIQAAG------QINNSGQIQIIPGTNQAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 167 ITP------SPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGgNVTLTLPVNNLVNASDTGAPTQLltespPTPL 240
Cdd:cd22540  155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 241 SKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 320
Cdd:cd22540  229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 321 LRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASraPHLSGTSKK 400
Cdd:cd22540  308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQV--TANNGTGTS 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 401 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 480
Cdd:cd22540  386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 578831275 481 QIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 526
Cdd:cd22540  466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
571-594 8.73e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 8.73e-07
                          10        20
                  ....*....|....*....|....
gi 578831275  571 ELQRHARTHTGDKRFECAQCQKRF 594
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
542-568 1.97e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.97e-05
                          10        20
                  ....*....|....*....|....*..
gi 578831275  542 LRAHVRLHTGERPFVCNwfFCGKRFTR 568
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 585-607 5.95e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 40.36  E-value: 5.95e-05
                          10        20
                  ....*....|....*....|...
gi 578831275  585 FECAQCQKRFMRSDHLTKHYKTH 607
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
449-587 1.76e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 449 VPVTITNTGGQQQLTVQNVSGNNLTISgLSPTQIQLQMEQALAGETQPGekrrrmactcPNCKDGEKRSGEQGKKKHvch 528
Cdd:COG5048  227 LPLTTNSQLSPKSLLSQSPSSLSSSDS-SSSASESPRSSLPTASSQSSS----------PNESDSSSEKGFSLPIKS--- 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578831275 529 iPDCGKTFRKTSLLRAHVR--LHTGE--RPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFEC 587
Cdd:COG5048  293 -KQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE 354
ZnF_C2H2 smart00355
zinc finger;
585-607 2.31e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.31e-03
                           10        20
                   ....*....|....*....|...
gi 578831275   585 FECAQCQKRFMRSDHLTKHYKTH 607
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
555-579 2.36e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.36e-03
                           10        20
                   ....*....|....*....|....*
gi 578831275   555 FVCNWffCGKRFTRSDELQRHARTH 579
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 527-603 8.86e-03

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


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 36.24  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  527 CHIPDCGKTFRKTSLLRAHVRLHTGE------RPFVCNWFFCGKRFTRSDELQRHARTHTGDKR-FECAQCQKRFMRSDH 599
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....
gi 578831275  600 LTKH 603
Cdd:pfam15909  82 LFKH 85
 
Name Accession Description Interval E-value
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 9-526 0e+00

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: 613.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275   9 AATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILS 88
Cdd:cd22540    1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  89 SKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKG--TRSNANIQYQAVPQIQASNsqtiqvQPNLTNQIQIIPGTNQAI 166
Cdd:cd22540   81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGsqTRSSTNQQYQISPQIQAAG------QINNSGQIQIIPGTNQAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 167 ITP------SPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGgNVTLTLPVNNLVNASDTGAPTQLltespPTPL 240
Cdd:cd22540  155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 241 SKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 320
Cdd:cd22540  229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 321 LRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASraPHLSGTSKK 400
Cdd:cd22540  308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQV--TANNGTGTS 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 401 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 480
Cdd:cd22540  386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 578831275 481 QIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 526
Cdd:cd22540  466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 19-524 7.96e-36

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: 143.13  E-value: 7.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  19 YLQPAASTTQDSQPSPLALLAATCSKIG-PPAVEAAVTPPAPPQPTPRKLVPIKPAP-----LPLSPGKNSFGIL----- 87
Cdd:cd22536    1 NKKGKTSGSQDSQPSPLALLAATCSKIGtPGENQGAGQQQQIIIDPSQGLVQLQNQPqqlelVTTQLAGNAWQIVaaapp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  88 SSKGNILQIQGSQLSASY-----------------PGGQLVFA------IQNPTMINkgtrSNANIQYQAVPQIQASNSQ 144
Cdd:cd22536   81 TSKENNVAQQGVSAATSSaapsssnngstsptkvkAGNSNASApgqfqvIQVQNMQN----PSGSVQYQVIPQIQTVEGQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 145 TIQVQPN-------LTNQIQIIP-GTNQAIITPSPSSHK-------------PVPIKPA---PIQKSSTTTTPVQSganV 200
Cdd:cd22536  157 QIQISPAnatalqdLQGQIQLIPaGNNQAILTTPNRTASgniiaqnlanqtvPVQIRPGvsiPLQLQTIPGAQAQV---V 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 201 VKLTGGGGNVTLTLPVNNLVNASdtGAPTQLLT--------------------------ESPPTPLSKTNKKArkKSLPA 254
Cdd:cd22536  234 TTLPINIGGVTLALPVINNVAAG--GGSGQLVQpsdggvsngnqlvstpittasvstmpESPSSSTTCTTTAS--TSLTS 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 255 SQPPVAVA----------------EQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPK----AEQQQVV 314
Cdd:cd22536  310 SDTLVSSAetgqyastaasserteEEPQTSAAESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQqiqiQQPQQQI 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 315 QIPQQALRVVQAASATLPTVPQKPSQNFQIQAAEpTPTQVYIR----TPSGEV--QTVLVQDSPPATAAATSNTTCSSPA 388
Cdd:cd22536  390 IQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVQ-SPTQVLIRaptlTPSGQIswQTVQVQNIQSLSNLQVQNAGLPQQL 468

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 389 SRAPHLSGTSKKHSAAIlrkerplPKIAPAGSIISLNAAQLAAAAQAMqTININ-----GVQVQGVPVTITNTGGQQQ-- 461
Cdd:cd22536  469 TLTPVSSSAGGTTIAQI-------APVAVAGTPITLNAAQLASVPNLQ-TVNVAnlgaaGVQVQGVPVTITSVAGQQQgq 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 462 --------------LTVQNVSgnNLTISGLSP---TQIQLQM-EQALAGETQPGEKRRRMACTCPNCKDGEKR-SGEQGK 522
Cdd:cd22536  541 dgvkvqqatiapvtVAVGNIA--NATIGAVSPdqiTQVQLQQaQQASDQEVQPGKRLRRVACSCPNCREGEGRgSSEPGK 618


                 ..
gi 578831275 523 KK 524
Cdd:cd22536  619 KK 620
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 24-524 8.19e-23

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: 101.90  E-value: 8.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  24 ASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLvpiKPAPLPLSPGKNSFGILSS-----------KGN 92
Cdd:cd22539    1 SSGGQESQPSPLALLAATCSRIESPNENSNSSQQQQQQQGELEL---DLTQAQIAQSANGWQIIPTgsqaptpskeqSGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  93 ILQIQGSQLSASYPGGQLVFA---IQNPTMINKGTRSNANIQYQAVPQIQASNSQTIQ-------VQPNLTNQIQIIPGT 162
Cdd:cd22539   78 SSTADSSKKSRVATAGYVVVAapnLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQfattqaqVQQDASGQLQIIPGT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 163 NQAIITPSPSS-----------HKPVPIKPAPIqKSSTTTTPVQSGANV-VKLTgggGNVTLtLPVNNLVNASDTGAPTQ 230
Cdd:cd22539  158 NQQIITTNRSGsgniitmpnllQQAVPIQGLGL-ANNVLPGQTQFVANVpVALN---GNITL-LPVSSVTASFFTNANSY 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 231 LLTESPPtplsktnkkarkkslpasqppvAVAEQVETVLIETtadNIIQAGnnllivqspgggqpavvqqvqvvppkaeq 310
Cdd:cd22539  233 STTTTTS----------------------NMGQQQQQILIQP---QLVQGG----------------------------- 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 311 qqvvqipqQALRVVQAASA-----TLPTVPQKPSQNFQIQAAePTPTQVYIRT---PSGEVQTVLVQDSPPATAAATSNT 382
Cdd:cd22539  259 --------QTIQALQAASLpgqtfTTQTISQEALQNLQIQTV-PNSGPIIIRTpvgPNGQVSWQTIQLQNLQTVTVNAAQ 329

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 383 TCSSPASRAPHLSgtskkhsaailrkerplpkiAPAGSIISLNaaqlaaaaqamqtiningvQVQGVPVTITNTGGQQ-- 460
Cdd:cd22539  330 LSSMPGLQTINLN--------------------ALGASGIQVH-------------------QLQGLPLTIANATGEHga 370

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578831275 461 QLTVQNVSGnnltiSGLSPTQIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKR-SGEQGKKK 524
Cdd:cd22539  371 QLGLHGAGG-----DGLHDDSAAEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRdSGDPGKKK 430
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 24-524 2.83e-21

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: 98.10  E-value: 2.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  24 ASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPrklVPIKPAPLPLSPGKNSFGILSS--------KGNILQ 95
Cdd:cd22537    1 GAAEQDTQPSPLALLAATCSKIGSPSPGDDAAAAGNAASAG---QTGDLASAQLTGAPNRWEVLTPtpttikdeAGNLVQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  96 IQGSQLSASypGGQLVFAIQ------NPTMINKGTRSNA---NIQYQAVPQIQASNSQTIQV----------QPNLTNQI 156
Cdd:cd22537   78 IPGGGTVTS--SGQYVLPLQslqnqqIFSVAPGSDASNGtvpNVQYQVIPQIQTTDGQQVQLgfatssdntgLQQEGGQI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 157 QIIPGTNQAIITPSPS---------SHKPVPIKPAPIQKSSTTTTpVQSGANVVklTGGGGNVTLtLPVNNL-------- 219
Cdd:cd22537  156 QIIPGSNQTIIASGTPsavqqllsqSGHVVQIQGVSIGGSSFPGQ-TQVVANVP--LGLPGNITF-VPINSVdldslgls 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 220 -----VNASDTgAPTQLL----------------TESPPTPLSKTNKKARKKSLPASQPPVAVAE----QVETVLIETTA 274
Cdd:cd22537  232 gtsqtMTTGIT-ADGQLIntgqavqssdnsgesgKVSPDINETNTNADLFVPTSSSSQLPVTIDStgilQQNASSLTTVS 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 275 DNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQI--------------PQQALRVVQAASATlpTVPQKPSQ 340
Cdd:cd22537  311 GQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHEsqqptsqaqivqgiTQQAIQGVQALGAQ--AIPQQALQ 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 341 NFQIQAAEPTP--TQVYIRTPSGEV--QTVLVQDSPPATAAatsnttcsspasrapHLSGTSKKHSAAILRKERPLPKIA 416
Cdd:cd22537  389 NLQLQLLNPGTflIQAQTVTPSGQItwQTFQVQGVQNLQNL---------------QIQNAPAQQITLTPVQTLTLGQVG 453

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 417 PAGSIISLNAAQLAAAAQAMQTININGV---QVQGVPVTITNTGGQQQLTV--------QNVSGNNLTISGLSPTQIQLq 485
Cdd:cd22537  454 AGGAITSTPVSLSTGQLPNLQTVTVNSIdsaGIQLQQSENADSPADIQIKEeepdseewQLSGDSTLNTNDLTHLRVQL- 532

                        570       580       590
                 ....*....|....*....|....*....|....*....
gi 578831275 486 MEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKK 524
Cdd:cd22537  533 VEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKK 571
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 481-529 2.16e-13

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: 65.93  E-value: 2.16e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578831275 481 QIQLQ-MEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHvcHI 529
Cdd:cd22545   35 NIQYQvIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQ--HI 82
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 24-51 2.74e-10

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: 57.07  E-value: 2.74e-10
                         10        20
                 ....*....|....*....|....*...
gi 578831275  24 ASTTQDSQPSPLALLAATCSKIGPPAVE 51
Cdd:cd22545    1 TSSAQDSQPSPLALLAATCSKIGSPAEN 28
zf-H2C2_2 pfam13465
Zinc-finger double domain;
571-594 8.73e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 8.73e-07
                          10        20
                  ....*....|....*....|....
gi 578831275  571 ELQRHARTHTGDKRFECAQCQKRF 594
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
542-568 1.97e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.97e-05
                          10        20
                  ....*....|....*....|....*..
gi 578831275  542 LRAHVRLHTGERPFVCNwfFCGKRFTR 568
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCP--ECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 585-607 5.95e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 40.36  E-value: 5.95e-05
                          10        20
                  ....*....|....*....|...
gi 578831275  585 FECAQCQKRFMRSDHLTKHYKTH 607
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 555-579 7.82e-05

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.98  E-value: 7.82e-05
                          10        20
                  ....*....|....*....|....*
gi 578831275  555 FVCNwfFCGKRFTRSDELQRHARTH 579
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 456-526 3.10e-04

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: 43.48  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 456 TGGQQQLTVQNVSGNNLTISGLSPtqiQLQME-------QALAGETQPGEKR-RRMACTCPNCKDGE-KRSGEQGKKKHV 526
Cdd:cd22553  308 TVVQQQAIQGNPLPPGTQIIAAGQ---QLQQDpndptkwQVVADGTPGSKKRlRRVACTCPNCRDGDgTRNGENKKKQHI 384
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
449-587 1.76e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275 449 VPVTITNTGGQQQLTVQNVSGNNLTISgLSPTQIQLQMEQALAGETQPGekrrrmactcPNCKDGEKRSGEQGKKKHvch 528
Cdd:COG5048  227 LPLTTNSQLSPKSLLSQSPSSLSSSDS-SSSASESPRSSLPTASSQSSS----------PNESDSSSEKGFSLPIKS--- 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578831275 529 iPDCGKTFRKTSLLRAHVR--LHTGE--RPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFEC 587
Cdd:COG5048  293 -KQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE 354
ZnF_C2H2 smart00355
zinc finger;
585-607 2.31e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.31e-03
                           10        20
                   ....*....|....*....|...
gi 578831275   585 FECAQCQKRFMRSDHLTKHYKTH 607
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
555-579 2.36e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.36e-03
                           10        20
                   ....*....|....*....|....*
gi 578831275   555 FVCNWffCGKRFTRSDELQRHARTH 579
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 527-603 8.86e-03

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


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 36.24  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831275  527 CHIPDCGKTFRKTSLLRAHVRLHTGE------RPFVCNWFFCGKRFTRSDELQRHARTHTGDKR-FECAQCQKRFMRSDH 599
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....
gi 578831275  600 LTKH 603
Cdd:pfam15909  82 LFKH 85
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 555-579 9.09e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.16  E-value: 9.09e-03
                          10        20
                  ....*....|....*....|....*
gi 578831275  555 FVCNwfFCGKRFTRSDELQRHARTH 579
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 585-607 9.09e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.16  E-value: 9.09e-03
                          10        20
                  ....*....|....*....|...
gi 578831275  585 FECAQCQKRFMRSDHLTKHYKTH 607
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 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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