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Conserved domains on  [gi|124504|sp|P13902|]
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RecName: Full=Protein INO4

Protein Classification

basic helix-loop-helix domain-containing protein( domain architecture ID 14413238)

basic helix-loop-helix (bHLH) domain-containing protein is a DNA-binding protein that may act as a transcription factor; similar to Saccharomyces cerevisiae protein INO4 that acts as transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.)

Gene Ontology:  GO:0003677
PubMed:  20219281

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLH_scINO4_like cd11403
basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar ...
 45-115 1.39e-32

basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar proteins; INO4 is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast. INO4 dimerizes with INO2 and binds to an UAS DNA element to control expression of the genes whose expression is inositol-responsive.


:

Pssm-ID: 381409  Cd Length: 71  Bit Score: 110.25  E-value: 1.39e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504    45 QIRINHVSSEKKRRELERAIFDELVAVVPDLQPQESRSELIIYLKSLSYLSWLYERNEKLRKQIIAKHEAK 115
Cdd:cd11403   1 QKKENHISSEHKRREAIREGFDRLCAIVPALSSSQSRSEAVVYVKTVEYLKELYERRAKLRSQLRSKGVEI 71
 
Name Accession Description Interval E-value
bHLH_scINO4_like cd11403
basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar ...
 45-115 1.39e-32

basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar proteins; INO4 is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast. INO4 dimerizes with INO2 and binds to an UAS DNA element to control expression of the genes whose expression is inositol-responsive.


Pssm-ID: 381409  Cd Length: 71  Bit Score: 110.25  E-value: 1.39e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504    45 QIRINHVSSEKKRRELERAIFDELVAVVPDLQPQESRSELIIYLKSLSYLSWLYERNEKLRKQIIAKHEAK 115
Cdd:cd11403   1 QKKENHISSEHKRREAIREGFDRLCAIVPALSSSQSRSEAVVYVKTVEYLKELYERRAKLRSQLRSKGVEI 71
HLH smart00353
helix loop helix domain;
53-103 3.05e-05

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 39.51  E-value: 3.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 124504       53 SEKKRRELERAIFDELVAVVPDLQPQESRSELIIYLKSLSYLSWLYERNEK 103
Cdd:smart00353   3 RERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
 
Name Accession Description Interval E-value
bHLH_scINO4_like cd11403
basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar ...
 45-115 1.39e-32

basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar proteins; INO4 is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast. INO4 dimerizes with INO2 and binds to an UAS DNA element to control expression of the genes whose expression is inositol-responsive.


Pssm-ID: 381409  Cd Length: 71  Bit Score: 110.25  E-value: 1.39e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504    45 QIRINHVSSEKKRRELERAIFDELVAVVPDLQPQESRSELIIYLKSLSYLSWLYERNEKLRKQIIAKHEAK 115
Cdd:cd11403   1 QKKENHISSEHKRREAIREGFDRLCAIVPALSSSQSRSEAVVYVKTVEYLKELYERRAKLRSQLRSKGVEI 71
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 45-115 1.11e-22

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription. The family also includes Saccharomyces cerevisiae INO4, which is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast.


Pssm-ID: 381410 [Multi-domain]  Cd Length: 70  Bit Score: 85.04  E-value: 1.11e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504    45 QIRINHVSSEKKRRELERAIFDELVAVVPDLQPQeSRSELIIYLKSLSYLSWLYERNEKLRKQIIAKHEAK 115
Cdd:cd11404   1 QRRLNHVRSEKKRRELIKKGYDELCALVPGLDPQ-KRTKADILQKAADWIQELKEENEKLEEQLDELKEAA 70
HLH smart00353
helix loop helix domain;
53-103 3.05e-05

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 39.51  E-value: 3.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 124504       53 SEKKRRELERAIFDELVAVVPDLQPQESRSELIIYLKSLSYLSWLYERNEK 103
Cdd:smart00353   3 RERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
bHLHzip_Mlx cd19687
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar ...
 47-108 4.15e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar proteins; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription.


Pssm-ID: 381530 [Multi-domain]  Cd Length: 76  Bit Score: 37.02  E-value: 4.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504    47 RINHVSSEKKRRELERAIFDELVAVVPDLQPQESR-----SELIIYLKSLSYLSWLYERNEKLRKQI 108
Cdd:cd19687   3 REAHTQAEQKRRDAIKKGYDDLQDIVPTCQQQDDIgsqklSKATILQRSIDYIQFLHQQKKKQEEEL 69
bHLHzip_MLXIP cd19688
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and ...
 47-108 9.35e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and similar proteins; MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm.


Pssm-ID: 381531  Cd Length: 72  Bit Score: 33.38  E-value: 9.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124504    47 RINHVSSEKKRRELERAIFDELVAVVPDLQPQESRSELIIYLKSLSYLSWL-------YERNEKLRKQI 108
Cdd:cd19688   4 RMKHISAEQKRRFNIKICFDTLNSLVSTLKNSKPISNAITLQKTVEYIAKLqqertqmQEETKRLREEI 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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