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Conserved domains on  [gi|15228207|ref|NP_190348|]
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basic helix-loop-helix (bHLH) DNA-binding superfamily protein [Arabidopsis thaliana]

Protein Classification

basic helix-loop-helix domain-containing protein( domain architecture ID 14413597)

basic helix-loop-helix (bHLH) domain-containing protein is a DNA-binding protein that may act as a transcription factor

CATH:  4.10.280.10
Gene Ontology:  GO:0003677|GO:0046983
PubMed:  20219281|15186484|1755826|8018712|19942615|12679534
SCOP:  4000913

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
 32-106 8.26e-28

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


:

Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 101.26  E-value: 8.26e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228207  32 KAVRERLKREHLNELFIELADTLELNQ-QNSGKASILCEATRFLKDVFGQIESLRKEHASLLSESSYVTTEKNELK 106
Cdd:cd11446   1 KACREKLRRDKLNERFMELSNVLEPGRpPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKAEKNELR 76
 
Name Accession Description Interval E-value
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
 32-106 8.26e-28

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 101.26  E-value: 8.26e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228207  32 KAVRERLKREHLNELFIELADTLELNQ-QNSGKASILCEATRFLKDVFGQIESLRKEHASLLSESSYVTTEKNELK 106
Cdd:cd11446   1 KACREKLRRDKLNERFMELSNVLEPGRpPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKAEKNELR 76
HLH smart00353
helix loop helix domain;
34-83 1.87e-04

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 38.35  E-value: 1.87e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15228207     34 VRERLKREHLNELFIELADTLELNQQNSG--KASILCEATRFLKDVFGQIES 83
Cdd:smart00353   2 ARERRRRRKINEAFDELRSLLPTLPKNKKlsKAEILRLAIEYIKSLQEELQK 53
HLH pfam00010
Helix-loop-helix DNA-binding domain;
28-76 1.66e-03

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 35.51  E-value: 1.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15228207    28 KRINKAVRERLKREHLNELFIELADTLELNQQNS--GKASILCEATRFLKD 76
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKklSKAEILRLAIEYIKH 51
 
Name Accession Description Interval E-value
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
 32-106 8.26e-28

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 101.26  E-value: 8.26e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228207  32 KAVRERLKREHLNELFIELADTLELNQ-QNSGKASILCEATRFLKDVFGQIESLRKEHASLLSESSYVTTEKNELK 106
Cdd:cd11446   1 KACREKLRRDKLNERFMELSNVLEPGRpPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKAEKNELR 76
HLH smart00353
helix loop helix domain;
34-83 1.87e-04

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 38.35  E-value: 1.87e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15228207     34 VRERLKREHLNELFIELADTLELNQQNSG--KASILCEATRFLKDVFGQIES 83
Cdd:smart00353   2 ARERRRRRKINEAFDELRSLLPTLPKNKKlsKAEILRLAIEYIKSLQEELQK 53
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 28-91 3.78e-04

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: 38.05  E-value: 3.78e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228207  28 KRINKAVRERLKREHLNELFIELADTL-ELNQQNSGKASILCEATRFLKDVFGQIESLRKEHASL 91
Cdd:cd11404   2 RRLNHVRSEKKRRELIKKGYDELCALVpGLDPQKRTKADILQKAADWIQELKEENEKLEEQLDEL 66
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
 29-91 4.62e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family; The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381525 [Multi-domain]  Cd Length: 65  Bit Score: 37.64  E-value: 4.62e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228207  29 RINKAVRERLKREHLNELFIELADTLELNqqNSGKAS---ILCEAtrflkdvFGQIESLRKEHASL 91
Cdd:cd19682   1 RLRHKKRERERRSELRELFDKLKQLLGLD--SDEKASklaVLTEA-------IEEIQQLKREEDEL 57
HLH pfam00010
Helix-loop-helix DNA-binding domain;
28-76 1.66e-03

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 35.51  E-value: 1.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15228207    28 KRINKAVRERLKREHLNELFIELADTLELNQQNS--GKASILCEATRFLKD 76
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKklSKAEILRLAIEYIKH 51
 
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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