Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Virtually nothing is known for this protein except that it has a decent cassette of znfC2H2 domains and a KRAB-domain
Description
Description:
zinc finger with KRAB and SCAN domains 8 [Source:HGNC Symbol;Acc:HGNC:12983]
Entrez Summary
TBA
Ensembl ID:
ENSG00000198315
External Link:
T044807_1.02
Interpro
IPR001909 ; IPR003309 ; IPR007087 ; IPR008916 ; IPR015880 ; ;
Protein Domain:
Protein: ENSP00000332750DBD: C2H2 ZF Containing ProteinsOther: KRAB, SCAN, SPXProtein: ENSP00000402948DBD: C2H2 ZF Containing ProteinsOther: KRAB, SCAN, SPX
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.
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"
Yes
GO-Info
GO:0003700 sequence-specific DNA binding transcription factor activity IBA - GO_REF:0000033
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
4a, two or more datasets predict it as a TF
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. 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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. 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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": 518, "scoreName": "E-value", "accession": "PF00096.24", "start": 518, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 540}}, {"startStyle": "curved", "end": 568, "endStyle": "curved", "aliStart": 546, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 568, "start": 546, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 568, "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": 546, "scoreName": "E-value", "accession": "PF00096.24", "start": 546, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 568}}, {"startStyle": "straight", "end": 134, "endStyle": "straight", "aliStart": 47, "text": "SCAN", "colour": "#9999ff", "aliEnd": 132, "start": 47, "href": "http://pfam.xfam.org/family/PF02023.15", "type": "pfama", "display": "true", "metadata": {"end": 134, "description": "The SCAN domain [1] (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several Pfam:PF00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerisation [2].", "database": "PfamA", "aliStart": 47, "scoreName": "E-value", "accession": "PF02023.15", "start": 47, "score": 1.6999999999999999e-37, "identifier": "SCAN domain", "type": "DBD", "aliEnd": 132}}, {"startStyle": "straight", "end": 259, "endStyle": "straight", "aliStart": 222, "text": "KRAB", "colour": "#9999ff", "aliEnd": 259, "start": 220, "href": "http://pfam.xfam.org/family/PF01352.25", "type": "pfama", "display": "true", "metadata": {"end": 259, "description": "The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions [2,3]. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation [4].", "database": "PfamA", "aliStart": 222, "scoreName": "E-value", "accession": "PF01352.25", "start": 220, "score": 3.5e-11, "identifier": "KRAB box", "type": "DBD", "aliEnd": 259}}, {"startStyle": "jagged", "end": 258, "endStyle": "jagged", "aliStart": 97, "text": "SPX", "colour": "#9999ff", "aliEnd": 248, "start": 3, "href": "http://pfam.xfam.org/family/PF03105.17", "type": "pfama", "display": "true", "metadata": {"end": 258, "description": "We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal [3]. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 Swiss:P17442 from Saccharomyces cerevisiae and NUC-2 Swiss:Q01317 from Neurospora crassa, are also members of this family [4,5]. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 [6] NUC-2 contains several ankyrin repeats Pfam:PF00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV) [1]. Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death [7]. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organisms [1,2,6,7]. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor [1].", "database": "PfamA", "aliStart": 97, "scoreName": "E-value", "accession": "PF03105.17", "start": 3, "score": 0.00016, "identifier": "SPX domain", "type": "DBD", "aliEnd": 248}}], "length": 579}
{"regions": [{"startStyle": "curved", "end": 344, "endStyle": "curved", "aliStart": 322, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 344, "start": 322, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 344, "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": 378, "scoreName": "E-value", "accession": "PF00096.24", "start": 378, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 400}}, {"startStyle": "curved", "end": 428, "endStyle": "curved", "aliStart": 406, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 428, "start": 406, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 428, "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": 406, "scoreName": "E-value", "accession": "PF00096.24", "start": 406, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 428}}, {"startStyle": "curved", "end": 456, "endStyle": "curved", "aliStart": 434, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 456, "start": 434, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 456, "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": 434, "scoreName": "E-value", "accession": "PF00096.24", "start": 434, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 456}}, {"startStyle": "curved", "end": 484, "endStyle": "curved", "aliStart": 462, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 484, "start": 462, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 484, "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": 462, "scoreName": "E-value", "accession": "PF00096.24", "start": 462, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 484}}, {"startStyle": "curved", "end": 512, "endStyle": "curved", "aliStart": 490, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 512, "start": 490, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 512, "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": 490, "scoreName": "E-value", "accession": "PF00096.24", "start": 490, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 512}}, {"startStyle": "curved", "end": 540, "endStyle": "curved", "aliStart": 518, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 540, "start": 518, "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. 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": 518, "scoreName": "E-value", "accession": "PF00096.24", "start": 518, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 540}}, {"startStyle": "curved", "end": 568, "endStyle": "curved", "aliStart": 546, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 568, "start": 546, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 568, "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": 546, "scoreName": "E-value", "accession": "PF00096.24", "start": 546, "score": 8.800000000000001e-59, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 568}}, {"startStyle": "straight", "end": 134, "endStyle": "straight", "aliStart": 47, "text": "SCAN", "colour": "#9999ff", "aliEnd": 132, "start": 47, "href": "http://pfam.xfam.org/family/PF02023.15", "type": "pfama", "display": "true", "metadata": {"end": 134, "description": "The SCAN domain [1] (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several Pfam:PF00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerisation [2].", "database": "PfamA", "aliStart": 47, "scoreName": "E-value", "accession": "PF02023.15", "start": 47, "score": 1.6999999999999999e-37, "identifier": "SCAN domain", "type": "DBD", "aliEnd": 132}}, {"startStyle": "straight", "end": 259, "endStyle": "straight", "aliStart": 222, "text": "KRAB", "colour": "#9999ff", "aliEnd": 259, "start": 220, "href": "http://pfam.xfam.org/family/PF01352.25", "type": "pfama", "display": "true", "metadata": {"end": 259, "description": "The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions [2,3]. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation [4].", "database": "PfamA", "aliStart": 222, "scoreName": "E-value", "accession": "PF01352.25", "start": 220, "score": 3.5e-11, "identifier": "KRAB box", "type": "DBD", "aliEnd": 259}}, {"startStyle": "jagged", "end": 258, "endStyle": "jagged", "aliStart": 97, "text": "SPX", "colour": "#9999ff", "aliEnd": 248, "start": 3, "href": "http://pfam.xfam.org/family/PF03105.17", "type": "pfama", "display": "true", "metadata": {"end": 258, "description": "We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal [3]. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 Swiss:P17442 from Saccharomyces cerevisiae and NUC-2 Swiss:Q01317 from Neurospora crassa, are also members of this family [4,5]. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 [6] NUC-2 contains several ankyrin repeats Pfam:PF00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV) [1]. Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death [7]. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organisms [1,2,6,7]. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor [1].", "database": "PfamA", "aliStart": 97, "scoreName": "E-value", "accession": "PF03105.17", "start": 3, "score": 0.00016, "identifier": "SPX domain", "type": "DBD", "aliEnd": 248}}], "length": 579}