Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Inferred motif
1 Monomer or homomultimer
In vivo/Misc source
Description
Description:
zinc finger E-box binding homeobox 2 [Source:HGNC Symbol;Acc:HGNC:14881]
Entrez Summary
#!usr/local/bin/perl
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The protein encoded by this gene is a member of the Zfh1 family of
2-handed zinc finger/homeodomain proteins. It is located in the nucleus and
functions as a DNA-binding transcriptional repressor that interacts with
activated SMADs. Mutations in this gene are associated with Hirschsprung
disease/Mowat-Wilson syndrome. Alternatively spliced transcript variants have
been found for this gene.[provided by RefSeq, Jan 2010]
Ensembl ID:
ENSG00000169554
External Link:
CisBP
Interpro
IPR001356 ; IPR007087 ; IPR008598 ; IPR009057 ; IPR015880 ; ;
Protein Domain:
ENSP00000302501
Protein Domain:
ENSP00000376601
Protein Domain:
ENSP00000395496
Protein Domain:
ENSP00000475329
Protein Domain:
ENSP00000454157
Protein Domain:
ENSP00000487174
Protein Domain:
ENSP00000394777
Protein Domain:
ENSP00000475502
Protein Domain:
ENSP00000443792
Protein Domain:
ENSP00000486240
Protein Domain:
ENSP00000490776
Protein Domain:
ENSP00000490508
Protein Domain:
ENSP00000490317
Protein Domain:
ENSP00000490141
Protein Domain:
ENSP00000490293
Protein Domain:
ENSP00000490872
Protein Domain:
ENSP00000489701
Protein Domain:
ENSP00000490723
Protein Domain:
ENSP00000490673
Protein Domain:
ENSP00000490934
Domain:
Protein: ENSP00000302501DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000376601DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000395496DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000475329DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000454157DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000487174DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000394777DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000475502DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000443792DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000486240DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000490776DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000490508DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000490317DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4Protein: ENSP00000490141DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000490293DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000490872DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000489701DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000490723DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000490673DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_2Protein: ENSP00000490934DBD: C2H2 ZF Containing ProteinsOther:
Previous Annotations
Source
Annotation
TF-CAT classification
TF Gene_DNA-Binding sequence-specific_DNA Binding Transactivation_ PMIDS:11430829 12714599
Vaquerizas 2009 TF classification
"a " Has direct evidence of TF function;
"b " Has evidence for an orthologous TF;
"c " contains likely DBDs, but has no functional evidence;
"x " is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription;
"other " category contains proteins without clear DBDs they curated from external sources.
a
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
Yes
GO-Info
GO:0001227 RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor IDA - PMID:20516212
Initial Assessment
1a1 Protein has a high confidence PWM (HT-SELEX, PBM or B1H model) or there is a crystal structure that supports sequence specific DNA binding;
1a2 There is high confidence data for a close ortholog (as defined in CisBP);
2a1 There is lower confidence direct evidence, such as a Jaspar, Hocomoco or Transfac model;
2a2 There is lower confidence evidence for an close ortholog;
3a There is decent circumstantial evidence for its role as a TF or not;
4a Two or more datasets predict it as a TF;
5a One of the source datasets predicts is as a TF
2a2, orthologous lower confidence evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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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. 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Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 651, "scoreName": "E-value", "accession": "PF00046.27", "start": 648, "score": 4.7e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 695}}, {"startStyle": "jagged", "end": 589, "endStyle": "straight", "aliStart": 573, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 589, "start": 570, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 589, "description": NaN, "database": "PfamA", "aliStart": 573, "scoreName": "E-value", "accession": "PF13465.4", "start": 570, "score": 9.699999999999999e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 589}}, {"startStyle": "straight", "end": 601, "endStyle": "straight", "aliStart": 580, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 600, "start": 580, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 601, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 580, "scoreName": "E-value", "accession": "PF13894.4", "start": 580, "score": 4.6e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 600}}], "length": 1214}
{"regions": [{"startStyle": "curved", "end": 262, "endStyle": "curved", "aliStart": 240, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 262, "start": 239, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 262, "description": "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. 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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 [2].", "database": "PfamA", "aliStart": 338, "scoreName": "E-value", "accession": "PF00096.24", "start": 338, "score": 1.5e-18, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 358}}], "length": 467}
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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 [2].", "database": "PfamA", "aliStart": 311, "scoreName": "E-value", "accession": "PF00096.24", "start": 311, "score": 3.7e-18, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 333}}, {"startStyle": "curved", "end": 360, "endStyle": "curved", "aliStart": 339, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 359, "start": 339, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 360, "description": "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 [2].", "database": "PfamA", "aliStart": 339, "scoreName": "E-value", "accession": "PF00096.24", "start": 339, "score": 3.7e-18, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 359}}, {"startStyle": "jagged", "end": 728, "endStyle": "curved", "aliStart": 681, "text": "HD", "colour": "#228B22", "aliEnd": 725, "start": 678, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 728, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 681, "scoreName": "E-value", "accession": "PF00046.27", "start": 678, "score": 4.7e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 725}}, {"startStyle": "jagged", "end": 619, "endStyle": "straight", "aliStart": 603, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 619, "start": 600, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 619, "description": NaN, "database": "PfamA", "aliStart": 603, "scoreName": "E-value", "accession": "PF13465.4", "start": 600, "score": 4.2999999999999995e-18, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 619}}, {"startStyle": "straight", "end": 631, "endStyle": "straight", "aliStart": 610, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 630, "start": 610, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 631, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 610, "scoreName": "E-value", "accession": "PF13894.4", "start": 610, "score": 3.7e-13, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 630}}], "length": 731}
{"regions": [{"startStyle": "curved", "end": 234, "endStyle": "curved", "aliStart": 212, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 234, "start": 211, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 234, "description": "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 [2].", "database": "PfamA", "aliStart": 212, "scoreName": "E-value", "accession": "PF00096.24", "start": 211, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 234}}, {"startStyle": "curved", "end": 263, "endStyle": "curved", "aliStart": 241, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 263, "start": 241, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 263, "description": "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 [2].", "database": "PfamA", "aliStart": 241, "scoreName": "E-value", "accession": "PF00096.24", "start": 241, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 263}}, {"startStyle": "curved", "end": 304, "endStyle": "curved", "aliStart": 282, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 304, "start": 282, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 304, "description": "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 [2].", "database": "PfamA", "aliStart": 282, "scoreName": "E-value", "accession": "PF00096.24", "start": 282, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 304}}, {"startStyle": "curved", "end": 331, "endStyle": "curved", "aliStart": 310, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 330, "start": 310, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": "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 [2].", "database": "PfamA", "aliStart": 310, "scoreName": "E-value", "accession": "PF00096.24", "start": 310, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 330}}, {"startStyle": "curved", "end": 1021, "endStyle": "curved", "aliStart": 999, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1021, "start": 999, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1021, "description": "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 [2].", "database": "PfamA", "aliStart": 999, "scoreName": "E-value", "accession": "PF00096.24", "start": 999, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1021}}, {"startStyle": "curved", "end": 1049, "endStyle": "curved", "aliStart": 1027, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1049, "start": 1027, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1049, "description": "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 [2].", "database": "PfamA", "aliStart": 1027, "scoreName": "E-value", "accession": "PF00096.24", "start": 1027, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1049}}, {"startStyle": "curved", "end": 1076, "endStyle": "curved", "aliStart": 1055, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1075, "start": 1055, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1076, "description": "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 [2].", "database": "PfamA", "aliStart": 1055, "scoreName": "E-value", "accession": "PF00096.24", "start": 1055, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1075}}, {"startStyle": "jagged", "end": 699, "endStyle": "curved", "aliStart": 652, "text": "HD", "colour": "#228B22", "aliEnd": 696, "start": 649, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 699, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 652, "scoreName": "E-value", "accession": "PF00046.27", "start": 649, "score": 4.7e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 696}}, {"startStyle": "jagged", "end": 590, "endStyle": "straight", "aliStart": 574, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 590, "start": 571, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 590, "description": NaN, "database": "PfamA", "aliStart": 574, "scoreName": "E-value", "accession": "PF13465.4", "start": 571, "score": 9.699999999999999e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 590}}, {"startStyle": "straight", "end": 602, "endStyle": "straight", "aliStart": 581, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 601, "start": 581, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 602, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 581, "scoreName": "E-value", "accession": "PF13894.4", "start": 581, "score": 4.6e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 601}}], "length": 1215}
{"regions": [{"startStyle": "curved", "end": 234, "endStyle": "curved", "aliStart": 212, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 234, "start": 211, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 234, "description": "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 [2].", "database": "PfamA", "aliStart": 212, "scoreName": "E-value", "accession": "PF00096.24", "start": 211, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 234}}, {"startStyle": "curved", "end": 263, "endStyle": "curved", "aliStart": 241, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 263, "start": 241, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 263, "description": "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 [2].", "database": "PfamA", "aliStart": 241, "scoreName": "E-value", "accession": "PF00096.24", "start": 241, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 263}}, {"startStyle": "curved", "end": 304, "endStyle": "curved", "aliStart": 282, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 304, "start": 282, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 304, "description": "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 [2].", "database": "PfamA", "aliStart": 282, "scoreName": "E-value", "accession": "PF00096.24", "start": 282, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 304}}, {"startStyle": "curved", "end": 331, "endStyle": "curved", "aliStart": 310, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 330, "start": 310, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": "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 [2].", "database": "PfamA", "aliStart": 310, "scoreName": "E-value", "accession": "PF00096.24", "start": 310, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 330}}, {"startStyle": "curved", "end": 1021, "endStyle": "curved", "aliStart": 999, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1021, "start": 999, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1021, "description": "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 [2].", "database": "PfamA", "aliStart": 999, "scoreName": "E-value", "accession": "PF00096.24", "start": 999, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1021}}, {"startStyle": "curved", "end": 1049, "endStyle": "curved", "aliStart": 1027, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1049, "start": 1027, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1049, "description": "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 [2].", "database": "PfamA", "aliStart": 1027, "scoreName": "E-value", "accession": "PF00096.24", "start": 1027, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1049}}, {"startStyle": "curved", "end": 1076, "endStyle": "curved", "aliStart": 1055, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1075, "start": 1055, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1076, "description": "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 [2].", "database": "PfamA", "aliStart": 1055, "scoreName": "E-value", "accession": "PF00096.24", "start": 1055, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1075}}, {"startStyle": "jagged", "end": 699, "endStyle": "curved", "aliStart": 652, "text": "HD", "colour": "#228B22", "aliEnd": 696, "start": 649, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 699, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 652, "scoreName": "E-value", "accession": "PF00046.27", "start": 649, "score": 4.7e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 696}}, {"startStyle": "jagged", "end": 590, "endStyle": "straight", "aliStart": 574, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 590, "start": 571, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 590, "description": NaN, "database": "PfamA", "aliStart": 574, "scoreName": "E-value", "accession": "PF13465.4", "start": 571, "score": 9.699999999999999e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 590}}, {"startStyle": "straight", "end": 602, "endStyle": "straight", "aliStart": 581, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 601, "start": 581, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 602, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 581, "scoreName": "E-value", "accession": "PF13894.4", "start": 581, "score": 4.6e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 601}}], "length": 1215}
{"regions": [{"startStyle": "curved", "end": 147, "endStyle": "curved", "aliStart": 125, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 147, "start": 124, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 147, "description": "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 [2].", "database": "PfamA", "aliStart": 125, "scoreName": "E-value", "accession": "PF00096.24", "start": 124, "score": 3.9e-16, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 147}}, {"startStyle": "curved", "end": 176, "endStyle": "curved", "aliStart": 154, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 176, "start": 154, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 176, "description": "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 [2].", "database": "PfamA", "aliStart": 154, "scoreName": "E-value", "accession": "PF00096.24", "start": 154, "score": 3.9e-16, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 176}}, {"startStyle": "curved", "end": 217, "endStyle": "curved", "aliStart": 195, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 217, "start": 195, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 217, "description": "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 [2].", "database": "PfamA", "aliStart": 195, "scoreName": "E-value", "accession": "PF00096.24", "start": 195, "score": 3.9e-16, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 217}}], "length": 221}
{"regions": [{"startStyle": "curved", "end": 210, "endStyle": "curved", "aliStart": 188, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 210, "start": 187, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 210, "description": "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 [2].", "database": "PfamA", "aliStart": 188, "scoreName": "E-value", "accession": "PF00096.24", "start": 187, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 210}}, {"startStyle": "curved", "end": 239, "endStyle": "curved", "aliStart": 217, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 239, "start": 217, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 239, "description": "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 [2].", "database": "PfamA", "aliStart": 217, "scoreName": "E-value", "accession": "PF00096.24", "start": 217, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 239}}, {"startStyle": "curved", "end": 280, "endStyle": "curved", "aliStart": 258, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 280, "start": 258, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 280, "description": "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 [2].", "database": "PfamA", "aliStart": 258, "scoreName": "E-value", "accession": "PF00096.24", "start": 258, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 280}}, {"startStyle": "curved", "end": 307, "endStyle": "curved", "aliStart": 286, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 306, "start": 286, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 307, "description": "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 [2].", "database": "PfamA", "aliStart": 286, "scoreName": "E-value", "accession": "PF00096.24", "start": 286, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 306}}, {"startStyle": "curved", "end": 997, "endStyle": "curved", "aliStart": 975, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 997, "start": 975, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 997, "description": "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 [2].", "database": "PfamA", "aliStart": 975, "scoreName": "E-value", "accession": "PF00096.24", "start": 975, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 997}}, {"startStyle": "curved", "end": 1025, "endStyle": "curved", "aliStart": 1003, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1025, "start": 1003, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1025, "description": "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 [2].", "database": "PfamA", "aliStart": 1003, "scoreName": "E-value", "accession": "PF00096.24", "start": 1003, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1025}}, {"startStyle": "curved", "end": 1052, "endStyle": "curved", "aliStart": 1031, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1051, "start": 1031, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1052, "description": "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 [2].", "database": "PfamA", "aliStart": 1031, "scoreName": "E-value", "accession": "PF00096.24", "start": 1031, "score": 5.5e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1051}}, {"startStyle": "jagged", "end": 675, "endStyle": "curved", "aliStart": 628, "text": "HD", "colour": "#228B22", "aliEnd": 672, "start": 625, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 675, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 628, "scoreName": "E-value", "accession": "PF00046.27", "start": 625, "score": 4.6e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 672}}, {"startStyle": "jagged", "end": 566, "endStyle": "straight", "aliStart": 550, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 566, "start": 547, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 566, "description": NaN, "database": "PfamA", "aliStart": 550, "scoreName": "E-value", "accession": "PF13465.4", "start": 547, "score": 8.099999999999999e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 566}}, {"startStyle": "straight", "end": 578, "endStyle": "straight", "aliStart": 557, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 577, "start": 557, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 578, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 557, "scoreName": "E-value", "accession": "PF13894.4", "start": 557, "score": 3.7999999999999996e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 577}}], "length": 1191}
{"regions": [{"startStyle": "curved", "end": 234, "endStyle": "curved", "aliStart": 212, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 234, "start": 211, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 234, "description": "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 [2].", "database": "PfamA", "aliStart": 212, "scoreName": "E-value", "accession": "PF00096.24", "start": 211, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 234}}, {"startStyle": "curved", "end": 263, "endStyle": "curved", "aliStart": 241, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 263, "start": 241, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 263, "description": "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 [2].", "database": "PfamA", "aliStart": 241, "scoreName": "E-value", "accession": "PF00096.24", "start": 241, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 263}}, {"startStyle": "curved", "end": 304, "endStyle": "curved", "aliStart": 282, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 304, "start": 282, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 304, "description": "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 [2].", "database": "PfamA", "aliStart": 282, "scoreName": "E-value", "accession": "PF00096.24", "start": 282, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 304}}, {"startStyle": "curved", "end": 331, "endStyle": "curved", "aliStart": 310, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 330, "start": 310, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": "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 [2].", "database": "PfamA", "aliStart": 310, "scoreName": "E-value", "accession": "PF00096.24", "start": 310, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 330}}, {"startStyle": "curved", "end": 1021, "endStyle": "curved", "aliStart": 999, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1021, "start": 999, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1021, "description": "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 [2].", "database": "PfamA", "aliStart": 999, "scoreName": "E-value", "accession": "PF00096.24", "start": 999, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1021}}, {"startStyle": "curved", "end": 1049, "endStyle": "curved", "aliStart": 1027, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1049, "start": 1027, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1049, "description": "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 [2].", "database": "PfamA", "aliStart": 1027, "scoreName": "E-value", "accession": "PF00096.24", "start": 1027, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1049}}, {"startStyle": "curved", "end": 1076, "endStyle": "curved", "aliStart": 1055, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1075, "start": 1055, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1076, "description": "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 [2].", "database": "PfamA", "aliStart": 1055, "scoreName": "E-value", "accession": "PF00096.24", "start": 1055, "score": 6e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1075}}, {"startStyle": "jagged", "end": 699, "endStyle": "curved", "aliStart": 652, "text": "HD", "colour": "#228B22", "aliEnd": 696, "start": 649, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 699, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 652, "scoreName": "E-value", "accession": "PF00046.27", "start": 649, "score": 4.2e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 696}}, {"startStyle": "jagged", "end": 590, "endStyle": "straight", "aliStart": 574, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 590, "start": 571, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 590, "description": NaN, "database": "PfamA", "aliStart": 574, "scoreName": "E-value", "accession": "PF13465.4", "start": 571, "score": 9.1e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 590}}, {"startStyle": "straight", "end": 602, "endStyle": "straight", "aliStart": 581, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 601, "start": 581, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 602, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 581, "scoreName": "E-value", "accession": "PF13894.4", "start": 581, "score": 4.2e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 601}}], "length": 1203}
{"regions": [{"startStyle": "curved", "end": 122, "endStyle": "curved", "aliStart": 100, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 122, "start": 99, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 122, "description": "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 [2].", "database": "PfamA", "aliStart": 100, "scoreName": "E-value", "accession": "PF00096.24", "start": 99, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 122}}, {"startStyle": "curved", "end": 151, "endStyle": "curved", "aliStart": 129, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 151, "start": 129, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 151, "description": "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 [2].", "database": "PfamA", "aliStart": 129, "scoreName": "E-value", "accession": "PF00096.24", "start": 129, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 151}}, {"startStyle": "curved", "end": 192, "endStyle": "curved", "aliStart": 170, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 192, "start": 170, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 192, "description": "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 [2].", "database": "PfamA", "aliStart": 170, "scoreName": "E-value", "accession": "PF00096.24", "start": 170, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 192}}, {"startStyle": "curved", "end": 219, "endStyle": "curved", "aliStart": 198, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 218, "start": 198, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 219, "description": "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 [2].", "database": "PfamA", "aliStart": 198, "scoreName": "E-value", "accession": "PF00096.24", "start": 198, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 218}}, {"startStyle": "curved", "end": 909, "endStyle": "curved", "aliStart": 887, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 909, "start": 887, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 909, "description": "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 [2].", "database": "PfamA", "aliStart": 887, "scoreName": "E-value", "accession": "PF00096.24", "start": 887, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 909}}, {"startStyle": "curved", "end": 937, "endStyle": "curved", "aliStart": 915, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 937, "start": 915, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 937, "description": "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 [2].", "database": "PfamA", "aliStart": 915, "scoreName": "E-value", "accession": "PF00096.24", "start": 915, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 937}}, {"startStyle": "curved", "end": 964, "endStyle": "curved", "aliStart": 943, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 963, "start": 943, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 964, "description": "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 [2].", "database": "PfamA", "aliStart": 943, "scoreName": "E-value", "accession": "PF00096.24", "start": 943, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 963}}, {"startStyle": "jagged", "end": 587, "endStyle": "curved", "aliStart": 540, "text": "HD", "colour": "#228B22", "aliEnd": 584, "start": 537, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 587, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 540, "scoreName": "E-value", "accession": "PF00046.27", "start": 537, "score": 3.9e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 584}}, {"startStyle": "jagged", "end": 478, "endStyle": "straight", "aliStart": 462, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 478, "start": 459, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 478, "description": NaN, "database": "PfamA", "aliStart": 462, "scoreName": "E-value", "accession": "PF13465.4", "start": 459, "score": 3.9999999999999997e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 478}}, {"startStyle": "straight", "end": 490, "endStyle": "straight", "aliStart": 469, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 489, "start": 469, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 490, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 469, "scoreName": "E-value", "accession": "PF13894.4", "start": 469, "score": 1.8999999999999998e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 489}}], "length": 1103}
{"regions": [{"startStyle": "curved", "end": 234, "endStyle": "curved", "aliStart": 212, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 234, "start": 211, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 234, "description": "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 [2].", "database": "PfamA", "aliStart": 212, "scoreName": "E-value", "accession": "PF00096.24", "start": 211, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 234}}, {"startStyle": "curved", "end": 263, "endStyle": "curved", "aliStart": 241, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 263, "start": 241, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 263, "description": "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 [2].", "database": "PfamA", "aliStart": 241, "scoreName": "E-value", "accession": "PF00096.24", "start": 241, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 263}}, {"startStyle": "curved", "end": 304, "endStyle": "curved", "aliStart": 282, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 304, "start": 282, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 304, "description": "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 [2].", "database": "PfamA", "aliStart": 282, "scoreName": "E-value", "accession": "PF00096.24", "start": 282, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 304}}, {"startStyle": "curved", "end": 356, "endStyle": "curved", "aliStart": 335, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 355, "start": 335, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 356, "description": "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 [2].", "database": "PfamA", "aliStart": 335, "scoreName": "E-value", "accession": "PF00096.24", "start": 335, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 355}}, {"startStyle": "curved", "end": 1046, "endStyle": "curved", "aliStart": 1024, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1046, "start": 1024, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1046, "description": "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 [2].", "database": "PfamA", "aliStart": 1024, "scoreName": "E-value", "accession": "PF00096.24", "start": 1024, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1046}}, {"startStyle": "curved", "end": 1074, "endStyle": "curved", "aliStart": 1052, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1074, "start": 1052, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1074, "description": "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 [2].", "database": "PfamA", "aliStart": 1052, "scoreName": "E-value", "accession": "PF00096.24", "start": 1052, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1074}}, {"startStyle": "curved", "end": 1101, "endStyle": "curved", "aliStart": 1080, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1100, "start": 1080, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1101, "description": "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 [2].", "database": "PfamA", "aliStart": 1080, "scoreName": "E-value", "accession": "PF00096.24", "start": 1080, "score": 8e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1100}}, {"startStyle": "jagged", "end": 724, "endStyle": "curved", "aliStart": 678, "text": "HD", "colour": "#228B22", "aliEnd": 721, "start": 674, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 724, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 678, "scoreName": "E-value", "accession": "PF00046.27", "start": 674, "score": 4.9e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 721}}, {"startStyle": "straight", "end": 627, "endStyle": "straight", "aliStart": 606, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 626, "start": 606, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 627, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 606, "scoreName": "E-value", "accession": "PF13894.4", "start": 606, "score": 5.599999999999999e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 626}}], "length": 1240}
{"regions": [{"startStyle": "curved", "end": 122, "endStyle": "curved", "aliStart": 100, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 122, "start": 99, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 122, "description": "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 [2].", "database": "PfamA", "aliStart": 100, "scoreName": "E-value", "accession": "PF00096.24", "start": 99, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 122}}, {"startStyle": "curved", "end": 151, "endStyle": "curved", "aliStart": 129, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 151, "start": 129, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 151, "description": "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 [2].", "database": "PfamA", "aliStart": 129, "scoreName": "E-value", "accession": "PF00096.24", "start": 129, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 151}}, {"startStyle": "curved", "end": 192, "endStyle": "curved", "aliStart": 170, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 192, "start": 170, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 192, "description": "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 [2].", "database": "PfamA", "aliStart": 170, "scoreName": "E-value", "accession": "PF00096.24", "start": 170, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 192}}, {"startStyle": "curved", "end": 219, "endStyle": "curved", "aliStart": 198, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 218, "start": 198, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 219, "description": "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 [2].", "database": "PfamA", "aliStart": 198, "scoreName": "E-value", "accession": "PF00096.24", "start": 198, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 218}}, {"startStyle": "curved", "end": 909, "endStyle": "curved", "aliStart": 887, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 909, "start": 887, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 909, "description": "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 [2].", "database": "PfamA", "aliStart": 887, "scoreName": "E-value", "accession": "PF00096.24", "start": 887, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 909}}, {"startStyle": "curved", "end": 937, "endStyle": "curved", "aliStart": 915, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 937, "start": 915, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 937, "description": "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 [2].", "database": "PfamA", "aliStart": 915, "scoreName": "E-value", "accession": "PF00096.24", "start": 915, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 937}}, {"startStyle": "curved", "end": 964, "endStyle": "curved", "aliStart": 943, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 963, "start": 943, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 964, "description": "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 [2].", "database": "PfamA", "aliStart": 943, "scoreName": "E-value", "accession": "PF00096.24", "start": 943, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 963}}, {"startStyle": "jagged", "end": 587, "endStyle": "curved", "aliStart": 540, "text": "HD", "colour": "#228B22", "aliEnd": 584, "start": 537, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 587, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 540, "scoreName": "E-value", "accession": "PF00046.27", "start": 537, "score": 3.9e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 584}}, {"startStyle": "jagged", "end": 478, "endStyle": "straight", "aliStart": 462, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 478, "start": 459, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 478, "description": NaN, "database": "PfamA", "aliStart": 462, "scoreName": "E-value", "accession": "PF13465.4", "start": 459, "score": 3.9999999999999997e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 478}}, {"startStyle": "straight", "end": 490, "endStyle": "straight", "aliStart": 469, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 489, "start": 469, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 490, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 469, "scoreName": "E-value", "accession": "PF13894.4", "start": 469, "score": 1.8999999999999998e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 489}}], "length": 1103}
{"regions": [{"startStyle": "curved", "end": 234, "endStyle": "curved", "aliStart": 212, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 234, "start": 211, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 234, "description": "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 [2].", "database": "PfamA", "aliStart": 212, "scoreName": "E-value", "accession": "PF00096.24", "start": 211, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 234}}, {"startStyle": "curved", "end": 263, "endStyle": "curved", "aliStart": 241, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 263, "start": 241, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 263, "description": "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 [2].", "database": "PfamA", "aliStart": 241, "scoreName": "E-value", "accession": "PF00096.24", "start": 241, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 263}}, {"startStyle": "curved", "end": 304, "endStyle": "curved", "aliStart": 282, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 304, "start": 282, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 304, "description": "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 [2].", "database": "PfamA", "aliStart": 282, "scoreName": "E-value", "accession": "PF00096.24", "start": 282, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 304}}, {"startStyle": "curved", "end": 331, "endStyle": "curved", "aliStart": 310, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 330, "start": 310, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": "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 [2].", "database": "PfamA", "aliStart": 310, "scoreName": "E-value", "accession": "PF00096.24", "start": 310, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 330}}, {"startStyle": "curved", "end": 1021, "endStyle": "curved", "aliStart": 999, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1021, "start": 999, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1021, "description": "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 [2].", "database": "PfamA", "aliStart": 999, "scoreName": "E-value", "accession": "PF00096.24", "start": 999, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1021}}, {"startStyle": "curved", "end": 1049, "endStyle": "curved", "aliStart": 1027, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1049, "start": 1027, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1049, "description": "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 [2].", "database": "PfamA", "aliStart": 1027, "scoreName": "E-value", "accession": "PF00096.24", "start": 1027, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1049}}, {"startStyle": "curved", "end": 1076, "endStyle": "curved", "aliStart": 1055, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1075, "start": 1055, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1076, "description": "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 [2].", "database": "PfamA", "aliStart": 1055, "scoreName": "E-value", "accession": "PF00096.24", "start": 1055, "score": 6.600000000000001e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1075}}, {"startStyle": "jagged", "end": 699, "endStyle": "curved", "aliStart": 652, "text": "HD", "colour": "#228B22", "aliEnd": 696, "start": 649, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 699, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 652, "scoreName": "E-value", "accession": "PF00046.27", "start": 649, "score": 4.7e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 696}}, {"startStyle": "jagged", "end": 590, "endStyle": "straight", "aliStart": 574, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 590, "start": 571, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 590, "description": NaN, "database": "PfamA", "aliStart": 574, "scoreName": "E-value", "accession": "PF13465.4", "start": 571, "score": 9.699999999999999e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 590}}, {"startStyle": "straight", "end": 602, "endStyle": "straight", "aliStart": 581, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 601, "start": 581, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 602, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 581, "scoreName": "E-value", "accession": "PF13894.4", "start": 581, "score": 4.6e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 601}}], "length": 1215}
{"regions": [{"startStyle": "curved", "end": 122, "endStyle": "curved", "aliStart": 100, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 122, "start": 99, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 122, "description": "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 [2].", "database": "PfamA", "aliStart": 100, "scoreName": "E-value", "accession": "PF00096.24", "start": 99, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 122}}, {"startStyle": "curved", "end": 151, "endStyle": "curved", "aliStart": 129, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 151, "start": 129, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 151, "description": "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 [2].", "database": "PfamA", "aliStart": 129, "scoreName": "E-value", "accession": "PF00096.24", "start": 129, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 151}}, {"startStyle": "curved", "end": 192, "endStyle": "curved", "aliStart": 170, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 192, "start": 170, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 192, "description": "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 [2].", "database": "PfamA", "aliStart": 170, "scoreName": "E-value", "accession": "PF00096.24", "start": 170, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 192}}, {"startStyle": "curved", "end": 219, "endStyle": "curved", "aliStart": 198, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 218, "start": 198, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 219, "description": "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 [2].", "database": "PfamA", "aliStart": 198, "scoreName": "E-value", "accession": "PF00096.24", "start": 198, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 218}}, {"startStyle": "curved", "end": 909, "endStyle": "curved", "aliStart": 887, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 909, "start": 887, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 909, "description": "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 [2].", "database": "PfamA", "aliStart": 887, "scoreName": "E-value", "accession": "PF00096.24", "start": 887, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 909}}, {"startStyle": "curved", "end": 937, "endStyle": "curved", "aliStart": 915, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 937, "start": 915, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 937, "description": "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 [2].", "database": "PfamA", "aliStart": 915, "scoreName": "E-value", "accession": "PF00096.24", "start": 915, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 937}}, {"startStyle": "curved", "end": 964, "endStyle": "curved", "aliStart": 943, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 963, "start": 943, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 964, "description": "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 [2].", "database": "PfamA", "aliStart": 943, "scoreName": "E-value", "accession": "PF00096.24", "start": 943, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 963}}, {"startStyle": "jagged", "end": 587, "endStyle": "curved", "aliStart": 540, "text": "HD", "colour": "#228B22", "aliEnd": 584, "start": 537, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 587, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 540, "scoreName": "E-value", "accession": "PF00046.27", "start": 537, "score": 3.9e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 584}}, {"startStyle": "jagged", "end": 478, "endStyle": "straight", "aliStart": 462, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 478, "start": 459, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 478, "description": NaN, "database": "PfamA", "aliStart": 462, "scoreName": "E-value", "accession": "PF13465.4", "start": 459, "score": 3.9999999999999997e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 478}}, {"startStyle": "straight", "end": 490, "endStyle": "straight", "aliStart": 469, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 489, "start": 469, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 490, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 469, "scoreName": "E-value", "accession": "PF13894.4", "start": 469, "score": 1.8999999999999998e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 489}}], "length": 1103}
{"regions": [{"startStyle": "curved", "end": 122, "endStyle": "curved", "aliStart": 100, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 122, "start": 99, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 122, "description": "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 [2].", "database": "PfamA", "aliStart": 100, "scoreName": "E-value", "accession": "PF00096.24", "start": 99, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 122}}, {"startStyle": "curved", "end": 151, "endStyle": "curved", "aliStart": 129, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 151, "start": 129, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 151, "description": "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 [2].", "database": "PfamA", "aliStart": 129, "scoreName": "E-value", "accession": "PF00096.24", "start": 129, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 151}}, {"startStyle": "curved", "end": 192, "endStyle": "curved", "aliStart": 170, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 192, "start": 170, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 192, "description": "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 [2].", "database": "PfamA", "aliStart": 170, "scoreName": "E-value", "accession": "PF00096.24", "start": 170, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 192}}, {"startStyle": "curved", "end": 219, "endStyle": "curved", "aliStart": 198, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 218, "start": 198, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 219, "description": "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 [2].", "database": "PfamA", "aliStart": 198, "scoreName": "E-value", "accession": "PF00096.24", "start": 198, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 218}}, {"startStyle": "curved", "end": 909, "endStyle": "curved", "aliStart": 887, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 909, "start": 887, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 909, "description": "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 [2].", "database": "PfamA", "aliStart": 887, "scoreName": "E-value", "accession": "PF00096.24", "start": 887, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 909}}, {"startStyle": "curved", "end": 937, "endStyle": "curved", "aliStart": 915, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 937, "start": 915, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 937, "description": "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 [2].", "database": "PfamA", "aliStart": 915, "scoreName": "E-value", "accession": "PF00096.24", "start": 915, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 937}}, {"startStyle": "curved", "end": 964, "endStyle": "curved", "aliStart": 943, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 963, "start": 943, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 964, "description": "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 [2].", "database": "PfamA", "aliStart": 943, "scoreName": "E-value", "accession": "PF00096.24", "start": 943, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 963}}, {"startStyle": "jagged", "end": 587, "endStyle": "curved", "aliStart": 540, "text": "HD", "colour": "#228B22", "aliEnd": 584, "start": 537, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 587, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 540, "scoreName": "E-value", "accession": "PF00046.27", "start": 537, "score": 3.9e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 584}}, {"startStyle": "jagged", "end": 478, "endStyle": "straight", "aliStart": 462, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 478, "start": 459, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 478, "description": NaN, "database": "PfamA", "aliStart": 462, "scoreName": "E-value", "accession": "PF13465.4", "start": 459, "score": 3.9999999999999997e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 478}}, {"startStyle": "straight", "end": 490, "endStyle": "straight", "aliStart": 469, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 489, "start": 469, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 490, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 469, "scoreName": "E-value", "accession": "PF13894.4", "start": 469, "score": 1.8999999999999998e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 489}}], "length": 1103}
{"regions": [{"startStyle": "curved", "end": 122, "endStyle": "curved", "aliStart": 100, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 122, "start": 99, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 122, "description": "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 [2].", "database": "PfamA", "aliStart": 100, "scoreName": "E-value", "accession": "PF00096.24", "start": 99, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 122}}, {"startStyle": "curved", "end": 151, "endStyle": "curved", "aliStart": 129, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 151, "start": 129, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 151, "description": "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 [2].", "database": "PfamA", "aliStart": 129, "scoreName": "E-value", "accession": "PF00096.24", "start": 129, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 151}}, {"startStyle": "curved", "end": 192, "endStyle": "curved", "aliStart": 170, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 192, "start": 170, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 192, "description": "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 [2].", "database": "PfamA", "aliStart": 170, "scoreName": "E-value", "accession": "PF00096.24", "start": 170, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 192}}, {"startStyle": "curved", "end": 219, "endStyle": "curved", "aliStart": 198, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 218, "start": 198, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 219, "description": "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 [2].", "database": "PfamA", "aliStart": 198, "scoreName": "E-value", "accession": "PF00096.24", "start": 198, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 218}}, {"startStyle": "curved", "end": 909, "endStyle": "curved", "aliStart": 887, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 909, "start": 887, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 909, "description": "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 [2].", "database": "PfamA", "aliStart": 887, "scoreName": "E-value", "accession": "PF00096.24", "start": 887, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 909}}, {"startStyle": "curved", "end": 937, "endStyle": "curved", "aliStart": 915, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 937, "start": 915, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 937, "description": "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 [2].", "database": "PfamA", "aliStart": 915, "scoreName": "E-value", "accession": "PF00096.24", "start": 915, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 937}}, {"startStyle": "curved", "end": 964, "endStyle": "curved", "aliStart": 943, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 963, "start": 943, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 964, "description": "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 [2].", "database": "PfamA", "aliStart": 943, "scoreName": "E-value", "accession": "PF00096.24", "start": 943, "score": 2.8000000000000003e-25, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 963}}, {"startStyle": "jagged", "end": 587, "endStyle": "curved", "aliStart": 540, "text": "HD", "colour": "#228B22", "aliEnd": 584, "start": 537, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 587, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 540, "scoreName": "E-value", "accession": "PF00046.27", "start": 537, "score": 3.9e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 584}}, {"startStyle": "jagged", "end": 478, "endStyle": "straight", "aliStart": 462, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 478, "start": 459, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 478, "description": NaN, "database": "PfamA", "aliStart": 462, "scoreName": "E-value", "accession": "PF13465.4", "start": 459, "score": 3.9999999999999997e-32, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 478}}, {"startStyle": "straight", "end": 490, "endStyle": "straight", "aliStart": 469, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 489, "start": 469, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 490, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 469, "scoreName": "E-value", "accession": "PF13894.4", "start": 469, "score": 1.8999999999999998e-16, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 489}}], "length": 1103}
{"regions": [{"startStyle": "curved", "end": 45, "endStyle": "curved", "aliStart": 23, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 45, "start": 23, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 45, "description": "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 [2].", "database": "PfamA", "aliStart": 23, "scoreName": "E-value", "accession": "PF00096.24", "start": 23, "score": 4.1e-17, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 45}}, {"startStyle": "curved", "end": 72, "endStyle": "curved", "aliStart": 51, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 71, "start": 51, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 72, "description": "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 [2].", "database": "PfamA", "aliStart": 51, "scoreName": "E-value", "accession": "PF00096.24", "start": 51, "score": 4.1e-17, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 71}}, {"startStyle": "curved", "end": 343, "endStyle": "curved", "aliStart": 322, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 342, "start": 322, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 343, "description": "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 [2].", "database": "PfamA", "aliStart": 322, "scoreName": "E-value", "accession": "PF00096.24", "start": 322, "score": 4.1e-17, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 342}}, {"startStyle": "curved", "end": 762, "endStyle": "curved", "aliStart": 740, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 762, "start": 740, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 762, "description": "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 [2].", "database": "PfamA", "aliStart": 740, "scoreName": "E-value", "accession": "PF00096.24", "start": 740, "score": 4.1e-17, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 762}}, {"startStyle": "curved", "end": 790, "endStyle": "curved", "aliStart": 768, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 790, "start": 768, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 790, "description": "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 [2].", "database": "PfamA", "aliStart": 768, "scoreName": "E-value", "accession": "PF00096.24", "start": 768, "score": 4.1e-17, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 790}}, {"startStyle": "curved", "end": 817, "endStyle": "curved", "aliStart": 796, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 816, "start": 796, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 817, "description": "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 [2].", "database": "PfamA", "aliStart": 796, "scoreName": "E-value", "accession": "PF00096.24", "start": 796, "score": 4.1e-17, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 816}}, {"startStyle": "jagged", "end": 440, "endStyle": "curved", "aliStart": 393, "text": "HD", "colour": "#228B22", "aliEnd": 437, "start": 390, "href": "http://pfam.xfam.org/family/PF00046.27", "type": "pfama", "display": "true", "metadata": {"end": 440, "description": "The homeobox domain or homeodomain was first identified in a number of drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, including vertebrates [PUBMED:2568852, PUBMED:1357790]. Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies [PUBMED:12445403]. The domain binds DNA through a helix-turn-helix (HTH) structure. ", "database": "PfamA", "aliStart": 393, "scoreName": "E-value", "accession": "PF00046.27", "start": 390, "score": 3.2e-05, "identifier": "Homeobox domain", "type": "DBD", "aliEnd": 437}}], "length": 956}