The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Likely to be sequence specific TF	1 Monomer or homomultimer	No motif	Has a putative AT-hook

Description

Description:	glyoxylate reductase 1 homolog
Entrez Summary	TBA
Ensembl ID:	ENSG00000140632
External Link:
Interpro	IPR000313; IPR006115; IPR008927; IPR029154;
Protein Domain:
Protein: ENSP00000322716	DBD: Other	Other: 2-Hacid_dh_C, 3HCDH_N, ApbA, F420_oxidored, NAD_bi
Protein: ENSP00000466570	DBD: Other	Other: 2-Hacid_dh_C, 3HCDH_N, ApbA, F420_oxidored, NAD_bi
Protein: ENSP00000468328	DBD: Other	Other: 2-Hacid_dh_C, 3HCDH_N, F420_oxidored, NAD_binding_
Protein: ENSP00000390276	DBD: Other	Other: 2-Hacid_dh_C, 3HCDH_N, ApbA, F420_oxidored, NAD_bi
Protein: ENSP00000467541	DBD: Other	Other:
Protein: ENSP00000467751	DBD: Other	Other: PWWP

Previous Annotations

Source	Annotation
TF-CAT classification	No PMIDS:
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.	x
CisBP considers it as a TF?	No
TFclass considers it as a TF?	No
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	5a, one of the source datasets predicts is as a TF
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence

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

{"regions": [{"startStyle": "straight", "end": 429, "endStyle": "straight", "aliStart": 269, "text": "NAD_binding_2", "colour": "#9999ff", "aliEnd": 425, "start": 269, "href": "http://pfam.xfam.org/family/PF03446.13", "type": "pfama", "display": "true", "metadata": {"end": 429, "description": "The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.", "database": "PfamA", "aliStart": 269, "scoreName": "E-value", "accession": "PF03446.13", "start": 269, "score": 6.999999999999999e-39, "identifier": "NAD binding domain of 6-phosphogluconate dehydrogenase", "type": "DBD", "aliEnd": 425}}, {"startStyle": "straight", "end": 551, "endStyle": "straight", "aliStart": 431, "text": "NAD_binding_11", "colour": "#9999ff", "aliEnd": 551, "start": 430, "href": "http://pfam.xfam.org/family/PF14833.4", "type": "pfama", "display": "true", "metadata": {"end": 551, "description": "3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure [1].", "database": "PfamA", "aliStart": 431, "scoreName": "E-value", "accession": "PF14833.4", "start": 430, "score": 5.799999999999999e-23, "identifier": "NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase", "type": "DBD", "aliEnd": 551}}, {"startStyle": "straight", "end": 91, "endStyle": "straight", "aliStart": 7, "text": "PWWP", "colour": "#9999ff", "aliEnd": 89, "start": 6, "href": "http://pfam.xfam.org/family/PF00855.15", "type": "pfama", "display": "true", "metadata": {"end": 91, "description": "The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif [1]. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyses all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression [2].", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00855.15", "start": 6, "score": 6.3e-19, "identifier": "PWWP domain", "type": "DBD", "aliEnd": 89}}, {"startStyle": "straight", "end": 362, "endStyle": "jagged", "aliStart": 269, "text": "F420_oxidored", "colour": "#9999ff", "aliEnd": 338, "start": 269, "href": "http://pfam.xfam.org/family/PF03807.15", "type": "pfama", "display": "true", "metadata": {"end": 362, "description": NaN, "database": "PfamA", "aliStart": 269, "scoreName": "E-value", "accession": "PF03807.15", "start": 269, "score": 9.9e-08, "identifier": "NADP oxidoreductase coenzyme F420-dependent", "type": "DBD", "aliEnd": 338}}, {"startStyle": "jagged", "end": 361, "endStyle": "jagged", "aliStart": 264, "text": "2-Hacid_dh_C", "colour": "#9999ff", "aliEnd": 339, "start": 234, "href": "http://pfam.xfam.org/family/PF02826.17", "type": "pfama", "display": "true", "metadata": {"end": 361, "description": "This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389.", "database": "PfamA", "aliStart": 264, "scoreName": "E-value", "accession": "PF02826.17", "start": 234, "score": 3.5e-05, "identifier": "D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 339}}, {"startStyle": "straight", "end": 361, "endStyle": "jagged", "aliStart": 266, "text": "Shikimate_DH", "colour": "#9999ff", "aliEnd": 310, "start": 258, "href": "http://pfam.xfam.org/family/PF01488.18", "type": "pfama", "display": "true", "metadata": {"end": 361, "description": "This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of  shikimate to 5-dehydroshikimate. This reaction is part of  the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of  quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.", "database": "PfamA", "aliStart": 266, "scoreName": "E-value", "accession": "PF01488.18", "start": 258, "score": 0.00023999999999999998, "identifier": "Shikimate / quinate 5-dehydrogenase", "type": "DBD", "aliEnd": 310}}, {"startStyle": "straight", "end": 342, "endStyle": "jagged", "aliStart": 270, "text": "ApbA", "colour": "#9999ff", "aliEnd": 331, "start": 270, "href": "http://pfam.xfam.org/family/PF02558.14", "type": "pfama", "display": "true", "metadata": {"end": 342, "description": "This is a family of 2-dehydropantoate 2-reductases also known as  ketopantoate reductases, EC:1.1.1.169.  The reaction catalysed by this  enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH.  AbpA catalyses the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway [2].  ApbA and PanE are allelic [2].  ApbA, the ketopantoate reductase enzyme is required for  the synthesis of thiamine via the APB biosynthetic pathway [1].", "database": "PfamA", "aliStart": 270, "scoreName": "E-value", "accession": "PF02558.14", "start": 270, "score": 0.00036, "identifier": "Ketopantoate reductase PanE/ApbA", "type": "DBD", "aliEnd": 331}}, {"startStyle": "straight", "end": 322, "endStyle": "jagged", "aliStart": 269, "text": "3HCDH_N", "colour": "#9999ff", "aliEnd": 304, "start": 269, "href": "http://pfam.xfam.org/family/PF02737.16", "type": "pfama", "display": "true", "metadata": {"end": 322, "description": "This family also includes lambda crystallin.", "database": "PfamA", "aliStart": 269, "scoreName": "E-value", "accession": "PF02737.16", "start": 269, "score": 0.003, "identifier": "3-hydroxyacyl-CoA dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 304}}], "length": 554}

{"regions": [{"startStyle": "straight", "end": 400, "endStyle": "straight", "aliStart": 240, "text": "NAD_binding_2", "colour": "#9999ff", "aliEnd": 396, "start": 240, "href": "http://pfam.xfam.org/family/PF03446.13", "type": "pfama", "display": "true", "metadata": {"end": 400, "description": "The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.", "database": "PfamA", "aliStart": 240, "scoreName": "E-value", "accession": "PF03446.13", "start": 240, "score": 6.2e-39, "identifier": "NAD binding domain of 6-phosphogluconate dehydrogenase", "type": "DBD", "aliEnd": 396}}, {"startStyle": "straight", "end": 522, "endStyle": "straight", "aliStart": 402, "text": "NAD_binding_11", "colour": "#9999ff", "aliEnd": 522, "start": 401, "href": "http://pfam.xfam.org/family/PF14833.4", "type": "pfama", "display": "true", "metadata": {"end": 522, "description": "3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure [1].", "database": "PfamA", "aliStart": 402, "scoreName": "E-value", "accession": "PF14833.4", "start": 401, "score": 6.099999999999999e-23, "identifier": "NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase", "type": "DBD", "aliEnd": 522}}, {"startStyle": "straight", "end": 79, "endStyle": "straight", "aliStart": 2, "text": "PWWP", "colour": "#9999ff", "aliEnd": 77, "start": 1, "href": "http://pfam.xfam.org/family/PF00855.15", "type": "pfama", "display": "true", "metadata": {"end": 79, "description": "The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif [1]. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyses all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression [2].", "database": "PfamA", "aliStart": 2, "scoreName": "E-value", "accession": "PF00855.15", "start": 1, "score": 4.7e-14, "identifier": "PWWP domain", "type": "DBD", "aliEnd": 77}}, {"startStyle": "straight", "end": 333, "endStyle": "jagged", "aliStart": 240, "text": "F420_oxidored", "colour": "#9999ff", "aliEnd": 309, "start": 240, "href": "http://pfam.xfam.org/family/PF03807.15", "type": "pfama", "display": "true", "metadata": {"end": 333, "description": NaN, "database": "PfamA", "aliStart": 240, "scoreName": "E-value", "accession": "PF03807.15", "start": 240, "score": 8.9e-08, "identifier": "NADP oxidoreductase coenzyme F420-dependent", "type": "DBD", "aliEnd": 309}}, {"startStyle": "jagged", "end": 332, "endStyle": "jagged", "aliStart": 235, "text": "2-Hacid_dh_C", "colour": "#9999ff", "aliEnd": 310, "start": 209, "href": "http://pfam.xfam.org/family/PF02826.17", "type": "pfama", "display": "true", "metadata": {"end": 332, "description": "This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389.", "database": "PfamA", "aliStart": 235, "scoreName": "E-value", "accession": "PF02826.17", "start": 209, "score": 3.3e-05, "identifier": "D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 310}}, {"startStyle": "straight", "end": 333, "endStyle": "jagged", "aliStart": 237, "text": "Shikimate_DH", "colour": "#9999ff", "aliEnd": 281, "start": 229, "href": "http://pfam.xfam.org/family/PF01488.18", "type": "pfama", "display": "true", "metadata": {"end": 333, "description": "This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of  shikimate to 5-dehydroshikimate. This reaction is part of  the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of  quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.", "database": "PfamA", "aliStart": 237, "scoreName": "E-value", "accession": "PF01488.18", "start": 229, "score": 0.00022999999999999998, "identifier": "Shikimate / quinate 5-dehydrogenase", "type": "DBD", "aliEnd": 281}}, {"startStyle": "straight", "end": 313, "endStyle": "jagged", "aliStart": 241, "text": "ApbA", "colour": "#9999ff", "aliEnd": 302, "start": 241, "href": "http://pfam.xfam.org/family/PF02558.14", "type": "pfama", "display": "true", "metadata": {"end": 313, "description": "This is a family of 2-dehydropantoate 2-reductases also known as  ketopantoate reductases, EC:1.1.1.169.  The reaction catalysed by this  enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH.  AbpA catalyses the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway [2].  ApbA and PanE are allelic [2].  ApbA, the ketopantoate reductase enzyme is required for  the synthesis of thiamine via the APB biosynthetic pathway [1].", "database": "PfamA", "aliStart": 241, "scoreName": "E-value", "accession": "PF02558.14", "start": 241, "score": 0.00033, "identifier": "Ketopantoate reductase PanE/ApbA", "type": "DBD", "aliEnd": 302}}, {"startStyle": "straight", "end": 293, "endStyle": "jagged", "aliStart": 240, "text": "3HCDH_N", "colour": "#9999ff", "aliEnd": 275, "start": 240, "href": "http://pfam.xfam.org/family/PF02737.16", "type": "pfama", "display": "true", "metadata": {"end": 293, "description": "This family also includes lambda crystallin.", "database": "PfamA", "aliStart": 240, "scoreName": "E-value", "accession": "PF02737.16", "start": 240, "score": 0.0028, "identifier": "3-hydroxyacyl-CoA dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 275}}], "length": 525}

{"regions": [{"startStyle": "straight", "end": 423, "endStyle": "straight", "aliStart": 269, "text": "NAD_binding_2", "colour": "#9999ff", "aliEnd": 419, "start": 269, "href": "http://pfam.xfam.org/family/PF03446.13", "type": "pfama", "display": "true", "metadata": {"end": 423, "description": "The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.", "database": "PfamA", "aliStart": 269, "scoreName": "E-value", "accession": "PF03446.13", "start": 269, "score": 1.7999999999999998e-33, "identifier": "NAD binding domain of 6-phosphogluconate dehydrogenase", "type": "DBD", "aliEnd": 419}}, {"startStyle": "straight", "end": 545, "endStyle": "straight", "aliStart": 425, "text": "NAD_binding_11", "colour": "#9999ff", "aliEnd": 545, "start": 424, "href": "http://pfam.xfam.org/family/PF14833.4", "type": "pfama", "display": "true", "metadata": {"end": 545, "description": "3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure [1].", "database": "PfamA", "aliStart": 425, "scoreName": "E-value", "accession": "PF14833.4", "start": 424, "score": 5.700000000000001e-23, "identifier": "NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase", "type": "DBD", "aliEnd": 545}}, {"startStyle": "straight", "end": 91, "endStyle": "straight", "aliStart": 7, "text": "PWWP", "colour": "#9999ff", "aliEnd": 89, "start": 6, "href": "http://pfam.xfam.org/family/PF00855.15", "type": "pfama", "display": "true", "metadata": {"end": 91, "description": "The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif [1]. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyses all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression [2].", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00855.15", "start": 6, "score": 6.2e-19, "identifier": "PWWP domain", "type": "DBD", "aliEnd": 89}}, {"startStyle": "straight", "end": 356, "endStyle": "jagged", "aliStart": 269, "text": "F420_oxidored", "colour": "#9999ff", "aliEnd": 326, "start": 269, "href": "http://pfam.xfam.org/family/PF03807.15", "type": "pfama", "display": "true", "metadata": {"end": 356, "description": NaN, "database": "PfamA", "aliStart": 269, "scoreName": "E-value", "accession": "PF03807.15", "start": 269, "score": 3.5e-05, "identifier": "NADP oxidoreductase coenzyme F420-dependent", "type": "DBD", "aliEnd": 326}}, {"startStyle": "jagged", "end": 354, "endStyle": "jagged", "aliStart": 264, "text": "2-Hacid_dh_C", "colour": "#9999ff", "aliEnd": 332, "start": 234, "href": "http://pfam.xfam.org/family/PF02826.17", "type": "pfama", "display": "true", "metadata": {"end": 354, "description": "This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389.", "database": "PfamA", "aliStart": 264, "scoreName": "E-value", "accession": "PF02826.17", "start": 234, "score": 0.00011999999999999999, "identifier": "D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 332}}, {"startStyle": "straight", "end": 326, "endStyle": "jagged", "aliStart": 266, "text": "Shikimate_DH", "colour": "#9999ff", "aliEnd": 303, "start": 258, "href": "http://pfam.xfam.org/family/PF01488.18", "type": "pfama", "display": "true", "metadata": {"end": 326, "description": "This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of  shikimate to 5-dehydroshikimate. This reaction is part of  the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of  quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.", "database": "PfamA", "aliStart": 266, "scoreName": "E-value", "accession": "PF01488.18", "start": 258, "score": 0.0018, "identifier": "Shikimate / quinate 5-dehydrogenase", "type": "DBD", "aliEnd": 303}}, {"startStyle": "straight", "end": 321, "endStyle": "jagged", "aliStart": 269, "text": "3HCDH_N", "colour": "#9999ff", "aliEnd": 302, "start": 269, "href": "http://pfam.xfam.org/family/PF02737.16", "type": "pfama", "display": "true", "metadata": {"end": 321, "description": "This family also includes lambda crystallin.", "database": "PfamA", "aliStart": 269, "scoreName": "E-value", "accession": "PF02737.16", "start": 269, "score": 0.0042, "identifier": "3-hydroxyacyl-CoA dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 302}}], "length": 548}

{"regions": [{"startStyle": "straight", "end": 349, "endStyle": "straight", "aliStart": 188, "text": "NAD_binding_2", "colour": "#9999ff", "aliEnd": 344, "start": 188, "href": "http://pfam.xfam.org/family/PF03446.13", "type": "pfama", "display": "true", "metadata": {"end": 349, "description": "The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.", "database": "PfamA", "aliStart": 188, "scoreName": "E-value", "accession": "PF03446.13", "start": 188, "score": 5.3e-39, "identifier": "NAD binding domain of 6-phosphogluconate dehydrogenase", "type": "DBD", "aliEnd": 344}}, {"startStyle": "straight", "end": 470, "endStyle": "straight", "aliStart": 350, "text": "NAD_binding_11", "colour": "#9999ff", "aliEnd": 470, "start": 349, "href": "http://pfam.xfam.org/family/PF14833.4", "type": "pfama", "display": "true", "metadata": {"end": 470, "description": "3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure [1].", "database": "PfamA", "aliStart": 350, "scoreName": "E-value", "accession": "PF14833.4", "start": 349, "score": 4.2e-23, "identifier": "NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase", "type": "DBD", "aliEnd": 470}}, {"startStyle": "straight", "end": 91, "endStyle": "straight", "aliStart": 7, "text": "PWWP", "colour": "#9999ff", "aliEnd": 89, "start": 6, "href": "http://pfam.xfam.org/family/PF00855.15", "type": "pfama", "display": "true", "metadata": {"end": 91, "description": "The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif [1]. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyses all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression [2].", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00855.15", "start": 6, "score": 2.7e-19, "identifier": "PWWP domain", "type": "DBD", "aliEnd": 89}}, {"startStyle": "straight", "end": 281, "endStyle": "jagged", "aliStart": 188, "text": "F420_oxidored", "colour": "#9999ff", "aliEnd": 257, "start": 188, "href": "http://pfam.xfam.org/family/PF03807.15", "type": "pfama", "display": "true", "metadata": {"end": 281, "description": NaN, "database": "PfamA", "aliStart": 188, "scoreName": "E-value", "accession": "PF03807.15", "start": 188, "score": 7.599999999999999e-08, "identifier": "NADP oxidoreductase coenzyme F420-dependent", "type": "DBD", "aliEnd": 257}}, {"startStyle": "jagged", "end": 280, "endStyle": "jagged", "aliStart": 183, "text": "2-Hacid_dh_C", "colour": "#9999ff", "aliEnd": 258, "start": 153, "href": "http://pfam.xfam.org/family/PF02826.17", "type": "pfama", "display": "true", "metadata": {"end": 280, "description": "This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389.", "database": "PfamA", "aliStart": 183, "scoreName": "E-value", "accession": "PF02826.17", "start": 153, "score": 2.4e-05, "identifier": "D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 258}}, {"startStyle": "straight", "end": 281, "endStyle": "jagged", "aliStart": 185, "text": "Shikimate_DH", "colour": "#9999ff", "aliEnd": 229, "start": 177, "href": "http://pfam.xfam.org/family/PF01488.18", "type": "pfama", "display": "true", "metadata": {"end": 281, "description": "This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of  shikimate to 5-dehydroshikimate. This reaction is part of  the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of  quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.", "database": "PfamA", "aliStart": 185, "scoreName": "E-value", "accession": "PF01488.18", "start": 177, "score": 0.00018999999999999998, "identifier": "Shikimate / quinate 5-dehydrogenase", "type": "DBD", "aliEnd": 229}}, {"startStyle": "straight", "end": 261, "endStyle": "jagged", "aliStart": 189, "text": "ApbA", "colour": "#9999ff", "aliEnd": 250, "start": 189, "href": "http://pfam.xfam.org/family/PF02558.14", "type": "pfama", "display": "true", "metadata": {"end": 261, "description": "This is a family of 2-dehydropantoate 2-reductases also known as  ketopantoate reductases, EC:1.1.1.169.  The reaction catalysed by this  enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH.  AbpA catalyses the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway [2].  ApbA and PanE are allelic [2].  ApbA, the ketopantoate reductase enzyme is required for  the synthesis of thiamine via the APB biosynthetic pathway [1].", "database": "PfamA", "aliStart": 189, "scoreName": "E-value", "accession": "PF02558.14", "start": 189, "score": 0.00028, "identifier": "Ketopantoate reductase PanE/ApbA", "type": "DBD", "aliEnd": 250}}, {"startStyle": "straight", "end": 241, "endStyle": "jagged", "aliStart": 188, "text": "3HCDH_N", "colour": "#9999ff", "aliEnd": 223, "start": 188, "href": "http://pfam.xfam.org/family/PF02737.16", "type": "pfama", "display": "true", "metadata": {"end": 241, "description": "This family also includes lambda crystallin.", "database": "PfamA", "aliStart": 188, "scoreName": "E-value", "accession": "PF02737.16", "start": 188, "score": 0.0028, "identifier": "3-hydroxyacyl-CoA dehydrogenase, NAD binding domain", "type": "DBD", "aliEnd": 223}}], "length": 473}

{"regions": [{"startStyle": "straight", "end": 91, "endStyle": "straight", "aliStart": 7, "text": "PWWP", "colour": "#9999ff", "aliEnd": 89, "start": 6, "href": "http://pfam.xfam.org/family/PF00855.15", "type": "pfama", "display": "true", "metadata": {"end": 91, "description": "The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif [1]. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyses all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression [2].", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00855.15", "start": 6, "score": 5e-20, "identifier": "PWWP domain", "type": "DBD", "aliEnd": 89}}], "length": 186}

TF Info Page for GLYR1 (AT hook)