The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	In vivo/Misc source	Only known motifs are from Transfac or HocoMoco - origin is uncertain

Description

Description:

zinc finger protein 423 [Source:HGNC Symbol;Acc:HGNC:16762]

Entrez Summary

The protein encoded by this gene is a nuclear protein that belongs to the family of Kruppel-like C2H2 zinc finger proteins. It functions as a DNA-binding transcription factor by using distinct zinc fingers in different signaling pathways. Thus, it is thought that this gene may have multiple roles in signal transduction during development. Mutations in this gene are associated with nephronophthisis-14 and Joubert syndrome-19. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2012]

Ensembl ID:

ENSG00000102935

External Link:

CisBP

Interpro

IPR007087; IPR015880;

Protein Domain:

ENSP00000262383

Protein Domain:

ENSP00000457664

Protein Domain:

ENSP00000455061

Protein Domain:

ENSP00000442321

Protein Domain:

ENSP00000479288

Domain:

Protein: ENSP00000262383	DBD: C2H2 ZF Containing Proteins	Other: zf-C2H2_2, zf-C2H2_4, zf-C2H2_6, zf-C2H2_jaz, zf-D
Protein: ENSP00000457664	DBD: C2H2 ZF Containing Proteins	Other: zf-C2H2_2, zf-C2H2_4, zf-C2H2_6, zf-C2H2_jaz, zf-D
Protein: ENSP00000455061	DBD: C2H2 ZF Containing Proteins	Other: zf-C2H2_2, zf-C2H2_4, zf-C2H2_6, zf-C2H2_jaz, zf-D
Protein: ENSP00000442321	DBD: C2H2 ZF Containing Proteins	Other: zf-C2H2_2, zf-C2H2_4, zf-C2H2_6, zf-C2H2_jaz, zf-D
Protein: ENSP00000479288	DBD: C2H2 ZF Containing Proteins	Other: C1_4, Zn-ribbon_8, zf-C2H2_4

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene_Transcription Factor Binding tf co-factor binding_TF PPI_ PMIDS:9151733 9774661
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.	b
CisBP considers it as a TF?	Yes
TFclass considers it as a TF?	Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"	No
GO-Info
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	2a1, Lower confidence direct evidence
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
Transfac	Transfac	License required	Direct
Misc	HocoMoco		Direct

Structure

Structure	PDB	Not_Covered

Experimental History

Method	Constructs
Tried in PBM? (Whether the protein was tried in PBM or not)
Tried in HT-SELEX (Whether the protein was tried in HT-SELEX or not, and if so, then what kind of clones were tested)
Other Information? (Tried with another method and failed?)

External Contribution

Name
Email
Comment
Reference

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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": 67, "scoreName": "E-value", "accession": "PF00096.24", "start": 67, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 86}}, {"startStyle": "curved", "end": 160, "endStyle": "curved", "aliStart": 138, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 160, "start": 138, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 160, "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 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": 194, "scoreName": "E-value", "accession": "PF00096.24", "start": 194, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 216}}, {"startStyle": "curved", "end": 244, "endStyle": "curved", "aliStart": 222, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 244, "start": 222, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 244, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. 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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": 222, "scoreName": "E-value", "accession": "PF00096.24", "start": 222, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 244}}, {"startStyle": "curved", "end": 286, "endStyle": "curved", "aliStart": 263, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 286, "start": 263, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 286, "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. 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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": 409, "scoreName": "E-value", "accession": "PF00096.24", "start": 409, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 433}}, {"startStyle": "curved", "end": 503, "endStyle": "curved", "aliStart": 480, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 503, "start": 480, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 503, "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": 480, "scoreName": "E-value", "accession": "PF00096.24", "start": 480, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 503}}, {"startStyle": "curved", "end": 540, "endStyle": "curved", "aliStart": 517, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 540, "start": 517, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 540, "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": 563, "scoreName": "E-value", "accession": "PF00096.24", "start": 563, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 588}}, {"startStyle": "curved", "end": 654, "endStyle": "curved", "aliStart": 632, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 654, "start": 632, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 654, "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": 632, "scoreName": "E-value", "accession": "PF00096.24", "start": 632, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 654}}, {"startStyle": "jagged", "end": 684, "endStyle": "curved", "aliStart": 664, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 684, "start": 663, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 684, "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": 664, "scoreName": "E-value", "accession": "PF00096.24", "start": 663, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 684}}, {"startStyle": "curved", "end": 715, "endStyle": "curved", "aliStart": 692, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 715, "start": 692, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 715, "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": 692, "scoreName": "E-value", "accession": "PF00096.24", "start": 692, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 715}}, {"startStyle": "curved", "end": 743, "endStyle": "curved", "aliStart": 720, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 743, "start": 720, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 743, "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": 720, "scoreName": "E-value", "accession": "PF00096.24", "start": 720, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 743}}, {"startStyle": "curved", "end": 773, "endStyle": "curved", "aliStart": 750, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 773, "start": 750, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 773, "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": 750, "scoreName": "E-value", "accession": "PF00096.24", "start": 750, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 773}}, {"startStyle": "curved", "end": 830, "endStyle": "curved", "aliStart": 807, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 830, "start": 807, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 830, "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": 807, "scoreName": "E-value", "accession": "PF00096.24", "start": 807, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 830}}, {"startStyle": "jagged", "end": 909, "endStyle": "curved", "aliStart": 888, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 909, "start": 886, "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": 888, "scoreName": "E-value", "accession": "PF00096.24", "start": 886, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 909}}, {"startStyle": "curved", "end": 952, "endStyle": "curved", "aliStart": 930, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 952, "start": 930, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 952, "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": 930, "scoreName": "E-value", "accession": "PF00096.24", "start": 930, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 952}}, {"startStyle": "curved", "end": 981, "endStyle": "curved", "aliStart": 959, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 981, "start": 959, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 981, "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": 959, "scoreName": "E-value", "accession": "PF00096.24", "start": 959, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 981}}, {"startStyle": "curved", "end": 1081, "endStyle": "jagged", "aliStart": 1064, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1081, "start": 1064, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1081, "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": 1064, "scoreName": "E-value", "accession": "PF00096.24", "start": 1064, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1081}}, {"startStyle": "curved", "end": 1143, "endStyle": "curved", "aliStart": 1121, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1143, "start": 1120, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1143, "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": 1121, "scoreName": "E-value", "accession": "PF00096.24", "start": 1120, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1143}}, {"startStyle": "curved", "end": 1252, "endStyle": "curved", "aliStart": 1229, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1252, "start": 1229, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1252, "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": 1229, "scoreName": "E-value", "accession": "PF00096.24", "start": 1229, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1252}}, {"startStyle": "curved", "end": 1282, "endStyle": "curved", "aliStart": 1259, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1282, "start": 1259, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1282, "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": 1259, "scoreName": "E-value", "accession": "PF00096.24", "start": 1259, "score": 2.9999999999999994e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1282}}, {"startStyle": "straight", "end": 346, "endStyle": "straight", "aliStart": 323, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 345, "start": 323, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 346, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 323, "scoreName": "E-value", "accession": "PF13894.4", "start": 323, "score": 4.799999999999999e-71, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 345}}, {"startStyle": "straight", "end": 464, "endStyle": "straight", "aliStart": 441, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 464, "start": 441, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 464, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 441, "scoreName": "E-value", "accession": "PF13894.4", "start": 441, "score": 4.799999999999999e-71, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 464}}, {"startStyle": "straight", "end": 804, "endStyle": "straight", "aliStart": 781, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 803, "start": 781, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 804, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 781, "scoreName": "E-value", "accession": "PF13894.4", "start": 781, "score": 4.799999999999999e-71, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 803}}, {"startStyle": "straight", "end": 1191, "endStyle": "straight", "aliStart": 1168, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 1190, "start": 1168, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 1191, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 1168, "scoreName": "E-value", "accession": "PF13894.4", "start": 1168, "score": 4.799999999999999e-71, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 1190}}, {"startStyle": "straight", "end": 1221, "endStyle": "straight", "aliStart": 1198, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 1220, "start": 1198, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 1221, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 1198, "scoreName": "E-value", "accession": "PF13894.4", "start": 1198, "score": 4.799999999999999e-71, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 1220}}, {"startStyle": "jagged", "end": 1209, "endStyle": "straight", "aliStart": 1186, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 1208, "start": 1184, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 1209, "description": NaN, "database": "PfamA", "aliStart": 1186, "scoreName": "E-value", "accession": "PF13465.4", "start": 1184, "score": 3.1e-25, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 1208}}, {"startStyle": "straight", "end": 806, "endStyle": "jagged", "aliStart": 782, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 803, "start": 779, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 806, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 782, "scoreName": "E-value", "accession": "PF05605.10", "start": 779, "score": 1.1e-22, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 803}}, {"startStyle": "straight", "end": 1044, "endStyle": "jagged", "aliStart": 989, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 1033, "start": 986, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 1044, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 989, "scoreName": "E-value", "accession": "PF05605.10", "start": 986, "score": 1.1e-22, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 1033}}, {"startStyle": "straight", "end": 466, "endStyle": "straight", "aliStart": 441, "text": "zf-C2H2_6", "colour": "#9999ff", "aliEnd": 464, "start": 440, "href": "http://pfam.xfam.org/family/PF13912.4", "type": "pfama", "display": "true", "metadata": {"end": 466, "description": NaN, "database": "PfamA", "aliStart": 441, "scoreName": "E-value", "accession": "PF13912.4", "start": 440, "score": 5.999999999999999e-20, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 464}}, {"startStyle": "straight", "end": 806, "endStyle": "straight", "aliStart": 780, "text": "zf-C2H2_6", "colour": "#9999ff", "aliEnd": 805, "start": 780, "href": "http://pfam.xfam.org/family/PF13912.4", "type": "pfama", "display": "true", "metadata": {"end": 806, "description": NaN, "database": "PfamA", "aliStart": 780, "scoreName": "E-value", "accession": "PF13912.4", "start": 780, "score": 5.999999999999999e-20, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 805}}, {"startStyle": "straight", "end": 805, "endStyle": "straight", "aliStart": 781, "text": "zfC2H2", "colour": "#9999ff", "aliEnd": 803, "start": 780, "href": "http://pfam.xfam.org/family/PF12171.6", "type": "pfama", "display": "true", "metadata": {"end": 805, "description": "This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localise in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localisation.", "database": "PfamA", "aliStart": 781, "scoreName": "E-value", "accession": "PF12171.6", "start": 780, "score": 1.1000000000000001e-18, "identifier": "Zinc-finger double-stranded RNA-binding", "type": "DBD", "aliEnd": 803}}, {"startStyle": "jagged", "end": 807, "endStyle": "jagged", "aliStart": 780, "text": "zf-C2H2_2", "colour": "#9999ff", "aliEnd": 803, "start": 772, "href": "http://pfam.xfam.org/family/PF12756.5", "type": "pfama", "display": "true", "metadata": {"end": 807, "description": "This family contains two copies of a C2H2-like zinc finger domain.", "database": "PfamA", "aliStart": 780, "scoreName": "E-value", "accession": "PF12756.5", "start": 772, "score": 3e-06, "identifier": "C2H2 type zinc-finger (2 copies)", "type": "DBD", "aliEnd": 803}}, {"startStyle": "straight", "end": 1008, "endStyle": "jagged", "aliStart": 989, "text": "zf-met", "colour": "#9999ff", "aliEnd": 1008, "start": 989, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 1008, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 989, "scoreName": "E-value", "accession": "PF12874.5", "start": 989, "score": 0.0006, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 1008}}, {"startStyle": "straight", "end": 1217, "endStyle": "jagged", "aliStart": 1199, "text": "zf-met", "colour": "#9999ff", "aliEnd": 1217, "start": 1198, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 1217, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 1199, "scoreName": "E-value", "accession": "PF12874.5", "start": 1198, "score": 0.0006, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 1217}}], "length": 1285}

{"regions": [{"startStyle": "curved", "end": 28, "endStyle": "curved", "aliStart": 7, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 26, "start": 7, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 28, "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": 7, "scoreName": "E-value", "accession": "PF00096.24", "start": 7, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 26}}, {"startStyle": "curved", "end": 100, "endStyle": "curved", "aliStart": 78, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 100, "start": 78, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 100, "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": 78, "scoreName": "E-value", "accession": "PF00096.24", "start": 78, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 100}}, {"startStyle": "curved", "end": 128, "endStyle": "curved", "aliStart": 106, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 128, "start": 106, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 128, "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": 106, "scoreName": "E-value", "accession": "PF00096.24", "start": 106, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 128}}, {"startStyle": "curved", "end": 156, "endStyle": "curved", "aliStart": 134, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 156, "start": 134, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 156, "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": 134, "scoreName": "E-value", "accession": "PF00096.24", "start": 134, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 156}}, {"startStyle": "curved", "end": 184, "endStyle": "curved", "aliStart": 162, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 184, "start": 162, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 184, "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": 162, "scoreName": "E-value", "accession": "PF00096.24", "start": 162, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 184}}, {"startStyle": "curved", "end": 226, "endStyle": "curved", "aliStart": 203, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 226, "start": 203, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 226, "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": 203, "scoreName": "E-value", "accession": "PF00096.24", "start": 203, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 226}}, {"startStyle": "curved", "end": 258, "endStyle": "curved", "aliStart": 236, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 258, "start": 235, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 258, "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": 236, "scoreName": "E-value", "accession": "PF00096.24", "start": 235, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 258}}, {"startStyle": "curved", "end": 373, "endStyle": "curved", "aliStart": 349, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 373, "start": 349, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 373, "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": 349, "scoreName": "E-value", "accession": "PF00096.24", "start": 349, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 373}}, {"startStyle": "curved", "end": 443, "endStyle": "curved", "aliStart": 420, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 443, "start": 420, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 443, "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": 420, "scoreName": "E-value", "accession": "PF00096.24", "start": 420, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 443}}, {"startStyle": "curved", "end": 480, "endStyle": "curved", "aliStart": 457, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 480, "start": 457, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 480, "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": 457, "scoreName": "E-value", "accession": "PF00096.24", "start": 457, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 480}}, {"startStyle": "curved", "end": 528, "endStyle": "curved", "aliStart": 503, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 528, "start": 503, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 528, "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": 503, "scoreName": "E-value", "accession": "PF00096.24", "start": 503, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 528}}, {"startStyle": "curved", "end": 594, "endStyle": "curved", "aliStart": 572, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 594, "start": 572, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 594, "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": 572, "scoreName": "E-value", "accession": "PF00096.24", "start": 572, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 594}}, {"startStyle": "jagged", "end": 624, "endStyle": "curved", "aliStart": 604, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 624, "start": 603, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 624, "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": 604, "scoreName": "E-value", "accession": "PF00096.24", "start": 603, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 624}}, {"startStyle": "curved", "end": 655, "endStyle": "curved", "aliStart": 632, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 655, "start": 632, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 655, "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": 632, "scoreName": "E-value", "accession": "PF00096.24", "start": 632, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 655}}, {"startStyle": "curved", "end": 683, "endStyle": "curved", "aliStart": 660, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 683, "start": 660, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 683, "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": 660, "scoreName": "E-value", "accession": "PF00096.24", "start": 660, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 683}}, {"startStyle": "curved", "end": 713, "endStyle": "curved", "aliStart": 690, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 713, "start": 690, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 713, "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": 690, "scoreName": "E-value", "accession": "PF00096.24", "start": 690, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 713}}, {"startStyle": "curved", "end": 770, "endStyle": "curved", "aliStart": 747, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 770, "start": 747, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 770, "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": 747, "scoreName": "E-value", "accession": "PF00096.24", "start": 747, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 770}}, {"startStyle": "jagged", "end": 849, "endStyle": "curved", "aliStart": 828, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 849, "start": 826, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 849, "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": 828, "scoreName": "E-value", "accession": "PF00096.24", "start": 826, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 849}}, {"startStyle": "curved", "end": 892, "endStyle": "curved", "aliStart": 870, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 892, "start": 870, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 892, "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": 870, "scoreName": "E-value", "accession": "PF00096.24", "start": 870, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 892}}, {"startStyle": "curved", "end": 921, "endStyle": "curved", "aliStart": 899, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 921, "start": 899, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 921, "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": 899, "scoreName": "E-value", "accession": "PF00096.24", "start": 899, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 921}}, {"startStyle": "curved", "end": 1021, "endStyle": "jagged", "aliStart": 1004, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1021, "start": 1004, "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": 1004, "scoreName": "E-value", "accession": "PF00096.24", "start": 1004, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1021}}, {"startStyle": "curved", "end": 1083, "endStyle": "curved", "aliStart": 1061, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1083, "start": 1060, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1083, "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": 1061, "scoreName": "E-value", "accession": "PF00096.24", "start": 1060, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1083}}, {"startStyle": "curved", "end": 1192, "endStyle": "curved", "aliStart": 1169, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1192, "start": 1169, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1192, "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": 1169, "scoreName": "E-value", "accession": "PF00096.24", "start": 1169, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1192}}, {"startStyle": "curved", "end": 1222, "endStyle": "curved", "aliStart": 1199, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1222, "start": 1199, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1222, "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": 1199, "scoreName": "E-value", "accession": "PF00096.24", "start": 1199, "score": 6.4e-58, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1222}}, {"startStyle": "straight", "end": 286, "endStyle": "straight", "aliStart": 263, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 285, "start": 263, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 286, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 263, "scoreName": "E-value", "accession": "PF13894.4", "start": 263, "score": 9.499999999999998e-72, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 285}}, {"startStyle": "straight", "end": 404, "endStyle": "straight", "aliStart": 381, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 404, "start": 381, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 404, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 381, "scoreName": "E-value", "accession": "PF13894.4", "start": 381, "score": 9.499999999999998e-72, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 404}}, {"startStyle": "straight", "end": 744, "endStyle": "straight", "aliStart": 721, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 743, "start": 721, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 744, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 721, "scoreName": "E-value", "accession": "PF13894.4", "start": 721, "score": 9.499999999999998e-72, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 743}}, {"startStyle": "straight", "end": 1131, "endStyle": "straight", "aliStart": 1108, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 1130, "start": 1108, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 1131, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 1108, "scoreName": "E-value", "accession": "PF13894.4", "start": 1108, "score": 9.499999999999998e-72, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 1130}}, {"startStyle": "straight", "end": 1161, "endStyle": "straight", "aliStart": 1138, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 1160, "start": 1138, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 1161, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 1138, "scoreName": "E-value", "accession": "PF13894.4", "start": 1138, "score": 9.499999999999998e-72, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 1160}}, {"startStyle": "jagged", "end": 1149, "endStyle": "straight", "aliStart": 1126, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 1148, "start": 1124, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 1149, "description": NaN, "database": "PfamA", "aliStart": 1126, "scoreName": "E-value", "accession": "PF13465.4", "start": 1124, "score": 1.5e-25, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 1148}}, {"startStyle": "straight", "end": 746, "endStyle": "jagged", "aliStart": 722, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 743, "start": 719, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 746, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 722, "scoreName": "E-value", "accession": "PF05605.10", "start": 719, "score": 2.2999999999999998e-23, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 743}}, {"startStyle": "straight", "end": 984, "endStyle": "jagged", "aliStart": 929, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 973, "start": 926, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 984, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 929, "scoreName": "E-value", "accession": "PF05605.10", "start": 926, "score": 2.2999999999999998e-23, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 973}}, {"startStyle": "straight", "end": 406, "endStyle": "straight", "aliStart": 381, "text": "zf-C2H2_6", "colour": "#9999ff", "aliEnd": 404, "start": 380, "href": "http://pfam.xfam.org/family/PF13912.4", "type": "pfama", "display": "true", "metadata": {"end": 406, "description": NaN, "database": "PfamA", "aliStart": 381, "scoreName": "E-value", "accession": "PF13912.4", "start": 380, "score": 2.0000000000000002e-20, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 404}}, {"startStyle": "straight", "end": 746, "endStyle": "straight", "aliStart": 720, "text": "zf-C2H2_6", "colour": "#9999ff", "aliEnd": 745, "start": 720, "href": "http://pfam.xfam.org/family/PF13912.4", "type": "pfama", "display": "true", "metadata": {"end": 746, "description": NaN, "database": "PfamA", "aliStart": 720, "scoreName": "E-value", "accession": "PF13912.4", "start": 720, "score": 2.0000000000000002e-20, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 745}}, {"startStyle": "straight", "end": 745, "endStyle": "straight", "aliStart": 721, "text": "zfC2H2", "colour": "#9999ff", "aliEnd": 743, "start": 720, "href": "http://pfam.xfam.org/family/PF12171.6", "type": "pfama", "display": "true", "metadata": {"end": 745, "description": "This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localise in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localisation.", "database": "PfamA", "aliStart": 721, "scoreName": "E-value", "accession": "PF12171.6", "start": 720, "score": 1.1000000000000002e-19, "identifier": "Zinc-finger double-stranded RNA-binding", "type": "DBD", "aliEnd": 743}}, {"startStyle": "jagged", "end": 747, "endStyle": "jagged", "aliStart": 720, "text": "zf-C2H2_2", "colour": "#9999ff", "aliEnd": 743, "start": 712, "href": "http://pfam.xfam.org/family/PF12756.5", "type": "pfama", "display": "true", "metadata": {"end": 747, "description": "This family contains two copies of a C2H2-like zinc finger domain.", "database": "PfamA", "aliStart": 720, "scoreName": "E-value", "accession": "PF12756.5", "start": 712, "score": 3.6000000000000003e-06, "identifier": "C2H2 type zinc-finger (2 copies)", "type": "DBD", "aliEnd": 743}}, {"startStyle": "straight", "end": 948, "endStyle": "jagged", "aliStart": 929, "text": "zf-met", "colour": "#9999ff", "aliEnd": 948, "start": 929, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 948, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 929, "scoreName": "E-value", "accession": "PF12874.5", "start": 929, "score": 0.0005200000000000001, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 948}}, {"startStyle": "straight", "end": 1157, "endStyle": "jagged", "aliStart": 1139, "text": "zf-met", "colour": "#9999ff", "aliEnd": 1157, "start": 1138, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 1157, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 1139, "scoreName": "E-value", "accession": "PF12874.5", "start": 1138, "score": 0.0005200000000000001, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 1157}}], "length": 1225}

{"regions": [{"startStyle": "curved", "end": 43, "endStyle": "curved", "aliStart": 21, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 43, "start": 21, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 43, "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": 21, "scoreName": "E-value", "accession": "PF00096.24", "start": 21, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 43}}, {"startStyle": "curved", "end": 71, "endStyle": "curved", "aliStart": 49, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 71, "start": 49, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 71, "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": 49, "scoreName": "E-value", "accession": "PF00096.24", "start": 49, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 71}}, {"startStyle": "curved", "end": 99, "endStyle": "curved", "aliStart": 77, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 99, "start": 77, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 99, "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": 77, "scoreName": "E-value", "accession": "PF00096.24", "start": 77, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 99}}, {"startStyle": "curved", "end": 127, "endStyle": "curved", "aliStart": 105, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 127, "start": 105, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 127, "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": 105, "scoreName": "E-value", "accession": "PF00096.24", "start": 105, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 127}}, {"startStyle": "curved", "end": 169, "endStyle": "curved", "aliStart": 146, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 169, "start": 146, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 169, "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": 146, "scoreName": "E-value", "accession": "PF00096.24", "start": 146, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 169}}, {"startStyle": "curved", "end": 201, "endStyle": "curved", "aliStart": 179, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 201, "start": 178, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 201, "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": 179, "scoreName": "E-value", "accession": "PF00096.24", "start": 178, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 201}}, {"startStyle": "curved", "end": 316, "endStyle": "curved", "aliStart": 292, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 316, "start": 292, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 316, "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": 292, "scoreName": "E-value", "accession": "PF00096.24", "start": 292, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 316}}, {"startStyle": "curved", "end": 386, "endStyle": "curved", "aliStart": 363, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 386, "start": 363, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 386, "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": 363, "scoreName": "E-value", "accession": "PF00096.24", "start": 363, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 386}}, {"startStyle": "curved", "end": 423, "endStyle": "curved", "aliStart": 400, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 423, "start": 400, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 423, "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": 400, "scoreName": "E-value", "accession": "PF00096.24", "start": 400, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 423}}, {"startStyle": "curved", "end": 471, "endStyle": "curved", "aliStart": 446, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 471, "start": 446, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 471, "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": 446, "scoreName": "E-value", "accession": "PF00096.24", "start": 446, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 471}}, {"startStyle": "curved", "end": 537, "endStyle": "curved", "aliStart": 515, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 537, "start": 515, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 537, "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": 515, "scoreName": "E-value", "accession": "PF00096.24", "start": 515, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 537}}, {"startStyle": "jagged", "end": 567, "endStyle": "curved", "aliStart": 547, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 567, "start": 546, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 567, "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": 547, "scoreName": "E-value", "accession": "PF00096.24", "start": 546, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 567}}, {"startStyle": "curved", "end": 598, "endStyle": "curved", "aliStart": 575, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 598, "start": 575, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 598, "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": 575, "scoreName": "E-value", "accession": "PF00096.24", "start": 575, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 598}}, {"startStyle": "curved", "end": 626, "endStyle": "curved", "aliStart": 603, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 626, "start": 603, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 626, "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": 603, "scoreName": "E-value", "accession": "PF00096.24", "start": 603, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 626}}, {"startStyle": "curved", "end": 656, "endStyle": "curved", "aliStart": 633, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 656, "start": 633, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 656, "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": 633, "scoreName": "E-value", "accession": "PF00096.24", "start": 633, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 656}}, {"startStyle": "curved", "end": 713, "endStyle": "curved", "aliStart": 690, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 713, "start": 690, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 713, "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": 690, "scoreName": "E-value", "accession": "PF00096.24", "start": 690, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 713}}, {"startStyle": "jagged", "end": 792, "endStyle": "curved", "aliStart": 771, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 792, "start": 769, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 792, "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": 771, "scoreName": "E-value", "accession": "PF00096.24", "start": 769, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 792}}, {"startStyle": "curved", "end": 835, "endStyle": "curved", "aliStart": 813, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 835, "start": 813, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 835, "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": 813, "scoreName": "E-value", "accession": "PF00096.24", "start": 813, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 835}}, {"startStyle": "curved", "end": 864, "endStyle": "curved", "aliStart": 842, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 864, "start": 842, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 864, "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": 842, "scoreName": "E-value", "accession": "PF00096.24", "start": 842, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 864}}, {"startStyle": "curved", "end": 964, "endStyle": "jagged", "aliStart": 947, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 964, "start": 947, "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": 947, "scoreName": "E-value", "accession": "PF00096.24", "start": 947, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 964}}, {"startStyle": "curved", "end": 1026, "endStyle": "curved", "aliStart": 1004, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1026, "start": 1003, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1026, "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": 1004, "scoreName": "E-value", "accession": "PF00096.24", "start": 1003, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1026}}, {"startStyle": "curved", "end": 1135, "endStyle": "curved", "aliStart": 1112, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1135, "start": 1112, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1135, "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": 1112, "scoreName": "E-value", "accession": "PF00096.24", "start": 1112, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1135}}, {"startStyle": "curved", "end": 1165, "endStyle": "curved", "aliStart": 1142, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1165, "start": 1142, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1165, "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": 1142, "scoreName": "E-value", "accession": "PF00096.24", "start": 1142, "score": 7.4e-57, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1165}}, {"startStyle": "straight", "end": 229, "endStyle": "straight", "aliStart": 206, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 228, "start": 206, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 229, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 206, "scoreName": "E-value", "accession": "PF13894.4", "start": 206, "score": 3.9999999999999993e-70, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 228}}, {"startStyle": "straight", "end": 347, "endStyle": "straight", "aliStart": 324, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 347, "start": 324, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 347, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 324, "scoreName": "E-value", "accession": "PF13894.4", "start": 324, "score": 3.9999999999999993e-70, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 347}}, {"startStyle": "straight", "end": 687, "endStyle": "straight", "aliStart": 664, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 686, "start": 664, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 687, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 664, "scoreName": "E-value", "accession": "PF13894.4", "start": 664, "score": 3.9999999999999993e-70, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 686}}, {"startStyle": "straight", "end": 1074, "endStyle": "straight", "aliStart": 1051, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 1073, "start": 1051, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 1074, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 1051, "scoreName": "E-value", "accession": "PF13894.4", "start": 1051, "score": 3.9999999999999993e-70, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 1073}}, {"startStyle": "straight", "end": 1104, "endStyle": "straight", "aliStart": 1081, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 1103, "start": 1081, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 1104, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 1081, "scoreName": "E-value", "accession": "PF13894.4", "start": 1081, "score": 3.9999999999999993e-70, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 1103}}, {"startStyle": "jagged", "end": 1092, "endStyle": "straight", "aliStart": 1069, "text": "zf-H2C2_2", "colour": "#9999ff", "aliEnd": 1091, "start": 1067, "href": "http://pfam.xfam.org/family/PF13465.4", "type": "pfama", "display": "true", "metadata": {"end": 1092, "description": NaN, "database": "PfamA", "aliStart": 1069, "scoreName": "E-value", "accession": "PF13465.4", "start": 1067, "score": 5.499999999999999e-26, "identifier": "Zinc-finger double domain", "type": "DBD", "aliEnd": 1091}}, {"startStyle": "straight", "end": 689, "endStyle": "jagged", "aliStart": 665, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 686, "start": 662, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 689, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 665, "scoreName": "E-value", "accession": "PF05605.10", "start": 662, "score": 4.0999999999999994e-25, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 686}}, {"startStyle": "straight", "end": 927, "endStyle": "jagged", "aliStart": 872, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 916, "start": 869, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 927, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 872, "scoreName": "E-value", "accession": "PF05605.10", "start": 869, "score": 4.0999999999999994e-25, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 916}}, {"startStyle": "straight", "end": 688, "endStyle": "straight", "aliStart": 664, "text": "zfC2H2", "colour": "#9999ff", "aliEnd": 686, "start": 663, "href": "http://pfam.xfam.org/family/PF12171.6", "type": "pfama", "display": "true", "metadata": {"end": 688, "description": "This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localise in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localisation.", "database": "PfamA", "aliStart": 664, "scoreName": "E-value", "accession": "PF12171.6", "start": 663, "score": 4.0000000000000004e-21, "identifier": "Zinc-finger double-stranded RNA-binding", "type": "DBD", "aliEnd": 686}}, {"startStyle": "straight", "end": 349, "endStyle": "straight", "aliStart": 324, "text": "zf-C2H2_6", "colour": "#9999ff", "aliEnd": 347, "start": 323, "href": "http://pfam.xfam.org/family/PF13912.4", "type": "pfama", "display": "true", "metadata": {"end": 349, "description": NaN, "database": "PfamA", "aliStart": 324, "scoreName": "E-value", "accession": "PF13912.4", "start": 323, "score": 2.3999999999999997e-19, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 347}}, {"startStyle": "straight", "end": 689, "endStyle": "straight", "aliStart": 663, "text": "zf-C2H2_6", "colour": "#9999ff", "aliEnd": 688, "start": 663, "href": "http://pfam.xfam.org/family/PF13912.4", "type": "pfama", "display": "true", "metadata": {"end": 689, "description": NaN, "database": "PfamA", "aliStart": 663, "scoreName": "E-value", "accession": "PF13912.4", "start": 663, "score": 2.3999999999999997e-19, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 688}}, {"startStyle": "jagged", "end": 689, "endStyle": "jagged", "aliStart": 663, "text": "zf-C2H2_2", "colour": "#9999ff", "aliEnd": 686, "start": 655, "href": "http://pfam.xfam.org/family/PF12756.5", "type": "pfama", "display": "true", "metadata": {"end": 689, "description": "This family contains two copies of a C2H2-like zinc finger domain.", "database": "PfamA", "aliStart": 663, "scoreName": "E-value", "accession": "PF12756.5", "start": 655, "score": 4.3e-08, "identifier": "C2H2 type zinc-finger (2 copies)", "type": "DBD", "aliEnd": 686}}, {"startStyle": "straight", "end": 891, "endStyle": "jagged", "aliStart": 872, "text": "zf-met", "colour": "#9999ff", "aliEnd": 891, "start": 872, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 891, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 872, "scoreName": "E-value", "accession": "PF12874.5", "start": 872, "score": 0.00039, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 891}}, {"startStyle": "straight", "end": 1100, "endStyle": "jagged", "aliStart": 1082, "text": "zf-met", "colour": "#9999ff", "aliEnd": 1100, "start": 1081, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 1100, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 1082, "scoreName": "E-value", "accession": "PF12874.5", "start": 1081, "score": 0.00039, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 1100}}], "length": 1168}

{"regions": [{"startStyle": "jagged", "end": 94, "endStyle": "jagged", "aliStart": 62, "text": "Zn-ribbon_8", "colour": "#9999ff", "aliEnd": 90, "start": 61, "href": "http://pfam.xfam.org/family/PF09723.8", "type": "pfama", "display": "true", "metadata": {"end": 94, "description": "This entry represents a region of about 41 amino acids found in a number of small proteins in a wide range of bacteria. The region usually begins with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One protein in this entry has been noted as a putative regulatory protein, designated FmdB. Most proteins in this entry have a C-terminal region containing highly degenerate sequence.", "database": "PfamA", "aliStart": 62, "scoreName": "E-value", "accession": "PF09723.8", "start": 61, "score": 0.0025, "identifier": "Zinc ribbon domain", "type": "DBD", "aliEnd": 90}}, {"startStyle": "straight", "end": 84, "endStyle": "jagged", "aliStart": 62, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 81, "start": 62, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 84, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 62, "scoreName": "E-value", "accession": "PF13894.4", "start": 62, "score": 0.0046, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 81}}, {"startStyle": "jagged", "end": 90, "endStyle": "straight", "aliStart": 47, "text": "C1_4", "colour": "#9999ff", "aliEnd": 88, "start": 28, "href": "http://pfam.xfam.org/family/PF07975.10", "type": "pfama", "display": "true", "metadata": {"end": 90, "description": "The carboxyl-terminal region of TFIIH is essential for transcription activity. This regions binds three zinc atoms through two independent domain. The first contains a C4 zinc finger motif, whereas the second is characterised by a CX(2)CX(2-4)FCADCD motif.  The solution structure of the second C-terminal domain revealed homology with the regulatory domain of protein kinase C (Pfam:PF00130) [1].", "database": "PfamA", "aliStart": 47, "scoreName": "E-value", "accession": "PF07975.10", "start": 28, "score": 0.0085, "identifier": "TFIIH C1-like domain", "type": "DBD", "aliEnd": 88}}], "length": 103}

TF Info Page for ZNF423 (C2H2 ZF(non-KRAB))

Conclusion

Description

Previous Annotations

DNA-Binding

Published Motif Data

Structure

Experimental History

External Contribution