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Conserved domains on  [gi|767995642|ref|XP_011523440|]
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transcription factor Sp2 isoform X3 [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 ...
 113-630 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: 632.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 113 AATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILS 192
Cdd:cd22540    1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 193 SKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKG--TRSNANIQYQAVPQIQASNsqtiqvQPNLTNQIQIIPGTNQAI 270
Cdd:cd22540   81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGsqTRSSTNQQYQISPQIQAAG------QINNSGQIQIIPGTNQAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 271 ITP------SPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGgNVTLTLPVNNLVNASDTGAPTQLltespPTPL 344
Cdd:cd22540  155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 345 SKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 424
Cdd:cd22540  229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 425 LRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASraPHLSGTSKK 504
Cdd:cd22540  308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQV--TANNGTGTS 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 505 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 584
Cdd:cd22540  386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 767995642 585 QIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 630
Cdd:cd22540  466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
675-698 9.92e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 9.92e-07
                          10        20
                  ....*....|....*....|....
gi 767995642  675 ELQRHARTHTGDKRFECAQCQKRF 698
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
646-672 2.23e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.23e-05
                          10        20
                  ....*....|....*....|....*..
gi 767995642  646 LRAHVRLHTGERPFVCNwfFCGKRFTR 672
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 ...
 689-711 6.76e-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: 6.76e-05
                          10        20
                  ....*....|....*....|...
gi 767995642  689 FECAQCQKRFMRSDHLTKHYKTH 711
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 ...
 113-630 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: 632.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 113 AATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILS 192
Cdd:cd22540    1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 193 SKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKG--TRSNANIQYQAVPQIQASNsqtiqvQPNLTNQIQIIPGTNQAI 270
Cdd:cd22540   81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGsqTRSSTNQQYQISPQIQAAG------QINNSGQIQIIPGTNQAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 271 ITP------SPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGgNVTLTLPVNNLVNASDTGAPTQLltespPTPL 344
Cdd:cd22540  155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 345 SKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 424
Cdd:cd22540  229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 425 LRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASraPHLSGTSKK 504
Cdd:cd22540  308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQV--TANNGTGTS 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 505 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 584
Cdd:cd22540  386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 767995642 585 QIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 630
Cdd:cd22540  466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
zf-H2C2_2 pfam13465
Zinc-finger double domain;
675-698 9.92e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 9.92e-07
                          10        20
                  ....*....|....*....|....
gi 767995642  675 ELQRHARTHTGDKRFECAQCQKRF 698
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
646-672 2.23e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.23e-05
                          10        20
                  ....*....|....*....|....*..
gi 767995642  646 LRAHVRLHTGERPFVCNwfFCGKRFTR 672
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 ...
 689-711 6.76e-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: 6.76e-05
                          10        20
                  ....*....|....*....|...
gi 767995642  689 FECAQCQKRFMRSDHLTKHYKTH 711
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
553-718 7.40e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 553 VPVTITNTGGQQQLTVQNVSGNNLTISgLSPTQIQLQMEQALAGETQPGekrrrmactcPNCKDGEKRSGEQGKKKHvch 632
Cdd:COG5048  227 LPLTTNSQLSPKSLLSQSPSSLSSSDS-SSSASESPRSSLPTASSQSSS----------PNESDSSSEKGFSLPIKS--- 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 633 iPDCGKTFRKTSLLRAHVR--LHTGE--RPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFEC--AQCQKRFMRSDH--- 703
Cdd:COG5048  293 -KQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNnep 371

                        170
                 ....*....|....*..
gi 767995642 704 --LTKHYKTHLVTKNFC 718
Cdd:COG5048  372 pqSLQQYKDLKNDKKSE 388
ZnF_C2H2 smart00355
zinc finger;
689-711 2.48e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.48e-03
                           10        20
                   ....*....|....*....|...
gi 767995642   689 FECAQCQKRFMRSDHLTKHYKTH 711
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
659-683 2.50e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|....*
gi 767995642   659 FVCNWffCGKRFTRSDELQRHARTH 683
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 631-707 8.97e-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: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642  631 CHIPDCGKTFRKTSLLRAHVRLHTGE------RPFVCNWFFCGKRFTRSDELQRHARTHTGDKR-FECAQCQKRFMRSDH 703
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....
gi 767995642  704 LTKH 707
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 ...
 113-630 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: 632.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 113 AATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILS 192
Cdd:cd22540    1 AATAAVSPSEYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLGPGKNSIGFLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 193 SKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKG--TRSNANIQYQAVPQIQASNsqtiqvQPNLTNQIQIIPGTNQAI 270
Cdd:cd22540   81 AKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGsqTRSSTNQQYQISPQIQAAG------QINNSGQIQIIPGTNQAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 271 ITP------SPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGgNVTLTLPVNNLVNASDTGAPTQLltespPTPL 344
Cdd:cd22540  155 ITPvqvlqqPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGG-NVALTLPVNNLVGTQDGATQLQL-----AAAP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 345 SKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQqA 424
Cdd:cd22540  229 SKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIPQQ-A 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 425 LRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASraPHLSGTSKK 504
Cdd:cd22540  308 LRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQV--TANNGTGTS 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 505 HSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPT 584
Cdd:cd22540  386 KPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQAIQTININGVQVQGVPVTITNAGGQQQLTVQTVSSNNLTISGLSPT 465

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 767995642 585 QIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHV 630
Cdd:cd22540  466 QIQLQMEQALEIETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHI 511
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 123-628 4.63e-38

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: 150.84  E-value: 4.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 123 YLQPAASTTQDSQPSPLALLAATCSKIG-PPAVEAAVTPPAPPQPTPRKLVPIK--PAPLPLSP---GKNSFGIL----- 191
Cdd:cd22536    1 NKKGKTSGSQDSQPSPLALLAATCSKIGtPGENQGAGQQQQIIIDPSQGLVQLQnqPQQLELVTtqlAGNAWQIVaaapp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 192 SSKGNILQIQGSQLSASY-----------------PGGQLVFA------IQNPTMINkgtrSNANIQYQAVPQIQASNSQ 248
Cdd:cd22536   81 TSKENNVAQQGVSAATSSaapsssnngstsptkvkAGNSNASApgqfqvIQVQNMQN----PSGSVQYQVIPQIQTVEGQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 249 TIQVQPN-------LTNQIQIIP-GTNQAIITPSPSSHK-------------PVPIKPA---PIQKSSTTTTPVQSganV 304
Cdd:cd22536  157 QIQISPAnatalqdLQGQIQLIPaGNNQAILTTPNRTASgniiaqnlanqtvPVQIRPGvsiPLQLQTIPGAQAQV---V 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 305 VKLTGGGGNVTLTLPVNNLVNASdtGAPTQLLT--------------------------ESPPTPLSKTNKKArkKSLPA 358
Cdd:cd22536  234 TTLPINIGGVTLALPVINNVAAG--GGSGQLVQpsdggvsngnqlvstpittasvstmpESPSSSTTCTTTAS--TSLTS 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 359 SQPPVAVA----------------EQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPK----AEQQQVV 418
Cdd:cd22536  310 SDTLVSSAetgqyastaasserteEEPQTSAAESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQqiqiQQPQQQI 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 419 QIPQQALRVVQAASATLPTVPQKPSQNFQIQAAEpTPTQVYIR----TPSGEV--QTVLVQDsppataAATSNTTCSSPA 492
Cdd:cd22536  390 IQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVQ-SPTQVLIRaptlTPSGQIswQTVQVQN------IQSLSNLQVQNA 462

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 493 SRAPHLSGTSKKHSAAilrkERPLPKIAP---AGSIISLNAAQLAAAAQAMqTININ-----GVQVQGVPVTITNTGGQQ 564
Cdd:cd22536  463 GLPQQLTLTPVSSSAG----GTTIAQIAPvavAGTPITLNAAQLASVPNLQ-TVNVAnlgaaGVQVQGVPVTITSVAGQQ 537

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 565 Q----------------LTVQNVSgnNLTISGLSP---TQIQLQM-EQALAGETQPGEKRRRMACTCPNCKDGEKR-SGE 623
Cdd:cd22536  538 QgqdgvkvqqatiapvtVAVGNIA--NATIGAVSPdqiTQVQLQQaQQASDQEVQPGKRLRRVACSCPNCREGEGRgSSE 615


                 ....*
gi 767995642 624 QGKKK 628
Cdd:cd22536  616 PGKKK 620
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 128-633 1.06e-24

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: 107.68  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 128 ASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLvpiKPAPLPLSPGKNSFGILSS-----------KGN 196
Cdd:cd22539    1 SSGGQESQPSPLALLAATCSRIESPNENSNSSQQQQQQQGELEL---DLTQAQIAQSANGWQIIPTgsqaptpskeqSGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 197 ILQIQGSQLSASYPGGQLVFA---IQNPTMINKGTRSNANIQYQAVPQIQASNSQTIQ-------VQPNLTNQIQIIPGT 266
Cdd:cd22539   78 SSTADSSKKSRVATAGYVVVAapnLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQfattqaqVQQDASGQLQIIPGT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 267 NQAIITPSPSS-----------HKPVPIKPAPIqKSSTTTTPVQSGANV-VKLTgggGNVTLtLPVNNLVNASDTGAPTQ 334
Cdd:cd22539  158 NQQIITTNRSGsgniitmpnllQQAVPIQGLGL-ANNVLPGQTQFVANVpVALN---GNITL-LPVSSVTASFFTNANSY 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 335 LLTESPPtplsktnkkarkkslpasqppvAVAEQVETVLIETtadNIIQAGnnllivqspgggqpavvqqvqvvppkaeq 414
Cdd:cd22539  233 STTTTTS----------------------NMGQQQQQILIQP---QLVQGG----------------------------- 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 415 qqvvqipqQALRVVQAASA-----TLPTVPQKPSQNFQIQAAePTPTQVYIRT---PSGEV--QTVLVQdsppataaats 484
Cdd:cd22539  259 --------QTIQALQAASLpgqtfTTQTISQEALQNLQIQTV-PNSGPIIIRTpvgPNGQVswQTIQLQ----------- 318

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 485 nttcsSPASRAPHLSGTSKkhsaailrkerplpkiAPAGSIISLNaaqlaaaaqamqTININGVQV---QGVPVTITNTG 561
Cdd:cd22539  319 -----NLQTVTVNAAQLSS----------------MPGLQTINLN------------ALGASGIQVhqlQGLPLTIANAT 365

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767995642 562 GQQ--QLTVQNVSGnnltiSGLSPTQIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKR-SGEQGKKKHvcHI 633
Cdd:cd22539  366 GEHgaQLGLHGAGG-----DGLHDDSAAEEGETEPDPQPQPGRRTRREACTCPYCKDGEGRdSGDPGKKKQ--HI 433
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 128-628 6.15e-23

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: 103.88  E-value: 6.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 128 ASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPrklVPIKPAPLPLSPGKNSFGILSS--------KGNILQ 199
Cdd:cd22537    1 GAAEQDTQPSPLALLAATCSKIGSPSPGDDAAAAGNAASAG---QTGDLASAQLTGAPNRWEVLTPtpttikdeAGNLVQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 200 IQGSQLSASypGGQLVFAIQ------NPTMINKGTRSNA---NIQYQAVPQIQASNSQTIQV----------QPNLTNQI 260
Cdd:cd22537   78 IPGGGTVTS--SGQYVLPLQslqnqqIFSVAPGSDASNGtvpNVQYQVIPQIQTTDGQQVQLgfatssdntgLQQEGGQI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 261 QIIPGTNQAIITPSPS---------SHKPVPIKPAPIQKSSTTTTpVQSGANVVklTGGGGNVTLtLPVNNL-------- 323
Cdd:cd22537  156 QIIPGSNQTIIASGTPsavqqllsqSGHVVQIQGVSIGGSSFPGQ-TQVVANVP--LGLPGNITF-VPINSVdldslgls 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 324 -----VNASDTgAPTQLL----------------TESPPTPLSKTNKKARKKSLPASQPPVAVAE----QVETVLIETTA 378
Cdd:cd22537  232 gtsqtMTTGIT-ADGQLIntgqavqssdnsgesgKVSPDINETNTNADLFVPTSSSSQLPVTIDStgilQQNASSLTTVS 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 379 DNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQI--------------PQQALRVVQAASATlpTVPQKPSQ 444
Cdd:cd22537  311 GQVHTSDLQGNYIQAPVSDETQAQNIQVSTAQPSVQQIQLHEsqqptsqaqivqgiTQQAIQGVQALGAQ--AIPQQALQ 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 445 NFQIQAAEPTP--TQVYIRTPSGEV--QTVLVQDSPPATAAatsnttcsspasrapHLSGTSKKHSAAILRKERPLPKIA 520
Cdd:cd22537  389 NLQLQLLNPGTflIQAQTVTPSGQItwQTFQVQGVQNLQNL---------------QIQNAPAQQITLTPVQTLTLGQVG 453

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 521 PAGSIISLNAAQLAAAAQAMQTININGV---QVQGVPVTITNTGGQQQLTV--------QNVSGNNLTISGLSPTQIQLq 589
Cdd:cd22537  454 AGGAITSTPVSLSTGQLPNLQTVTVNSIdsaGIQLQQSENADSPADIQIKEeepdseewQLSGDSTLNTNDLTHLRVQL- 532

                        570       580       590
                 ....*....|....*....|....*....|....*....
gi 767995642 590 MEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKK 628
Cdd:cd22537  533 VEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKK 571
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 585-633 1.69e-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: 66.31  E-value: 1.69e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767995642 585 QIQLQ-MEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHvcHI 633
Cdd:cd22545   35 NIQYQvIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQ--HI 82
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 128-155 2.32e-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: 57.45  E-value: 2.32e-10
                         10        20
                 ....*....|....*....|....*...
gi 767995642 128 ASTTQDSQPSPLALLAATCSKIGPPAVE 155
Cdd:cd22545    1 TSSAQDSQPSPLALLAATCSKIGSPAEN 28
zf-H2C2_2 pfam13465
Zinc-finger double domain;
675-698 9.92e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.44  E-value: 9.92e-07
                          10        20
                  ....*....|....*....|....
gi 767995642  675 ELQRHARTHTGDKRFECAQCQKRF 698
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
646-672 2.23e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.23e-05
                          10        20
                  ....*....|....*....|....*..
gi 767995642  646 LRAHVRLHTGERPFVCNwfFCGKRFTR 672
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 ...
 689-711 6.76e-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: 6.76e-05
                          10        20
                  ....*....|....*....|...
gi 767995642  689 FECAQCQKRFMRSDHLTKHYKTH 711
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
553-718 7.40e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 553 VPVTITNTGGQQQLTVQNVSGNNLTISgLSPTQIQLQMEQALAGETQPGekrrrmactcPNCKDGEKRSGEQGKKKHvch 632
Cdd:COG5048  227 LPLTTNSQLSPKSLLSQSPSSLSSSDS-SSSASESPRSSLPTASSQSSS----------PNESDSSSEKGFSLPIKS--- 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 633 iPDCGKTFRKTSLLRAHVR--LHTGE--RPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFEC--AQCQKRFMRSDH--- 703
Cdd:COG5048  293 -KQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNnep 371

                        170
                 ....*....|....*..
gi 767995642 704 --LTKHYKTHLVTKNFC 718
Cdd:COG5048  372 pqSLQQYKDLKNDKKSE 388
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 560-630 8.64e-05

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: 45.40  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642 560 TGGQQQLTVQNVSGNNLTISGLSPtqiQLQME-------QALAGETQPGEKR-RRMACTCPNCKDGE-KRSGEQGKKKHV 630
Cdd:cd22553  308 TVVQQQAIQGNPLPPGTQIIAAGQ---QLQQDpndptkwQVVADGTPGSKKRlRRVACTCPNCRDGDgTRNGENKKKQHI 384
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 659-683 8.89e-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: 8.89e-05
                          10        20
                  ....*....|....*....|....*
gi 767995642  659 FVCNwfFCGKRFTRSDELQRHARTH 683
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
689-711 2.48e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.48e-03
                           10        20
                   ....*....|....*....|...
gi 767995642   689 FECAQCQKRFMRSDHLTKHYKTH 711
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
659-683 2.50e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|....*
gi 767995642   659 FVCNWffCGKRFTRSDELQRHARTH 683
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 631-707 8.97e-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: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995642  631 CHIPDCGKTFRKTSLLRAHVRLHTGE------RPFVCNWFFCGKRFTRSDELQRHARTHTGDKR-FECAQCQKRFMRSDH 703
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81


                  ....
gi 767995642  704 LTKH 707
Cdd:pfam15909  82 LFKH 85
 
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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