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Conserved domains on  [gi|821324807|ref|NP_001295567|]
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max-interacting protein 1 isoform 2 [Danio rerio]

Protein Classification

basic helix-loop-helix domain-containing protein( domain architecture ID 385)

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
SCOP:  4000913

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLH_SF super family cl00081
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 56-127 3.51e-39

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


The actual alignment was detected with superfamily member cd18930:

Pssm-ID: 469605 [Multi-domain]  Cd Length: 80  Bit Score: 130.12  E-value: 3.51e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821324807  56 YRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRH 127
Cdd:cd18930    1 NRSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRF 72
 
Name Accession Description Interval E-value
bHLHzip_MXI1 cd18930
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and ...
 56-127 3.51e-39

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and similar proteins; MXI1, also termed Max interactor 1, or Class C basic helix-loop-helix protein 11 (bHLHc11), is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX. It plays an important role in the regulation of cell proliferation.


Pssm-ID: 381500 [Multi-domain]  Cd Length: 80  Bit Score: 130.12  E-value: 3.51e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821324807  56 YRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRH 127
Cdd:cd18930    1 NRSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRF 72
HLH pfam00010
Helix-loop-helix DNA-binding domain;
56-108 3.64e-11

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 56.31  E-value: 3.64e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 821324807   56 YRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLE 108
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
61-113 1.34e-10

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 54.92  E-value: 1.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 821324807    61 NELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRK 113
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
 
Name Accession Description Interval E-value
bHLHzip_MXI1 cd18930
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and ...
 56-127 3.51e-39

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and similar proteins; MXI1, also termed Max interactor 1, or Class C basic helix-loop-helix protein 11 (bHLHc11), is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX. It plays an important role in the regulation of cell proliferation.


Pssm-ID: 381500 [Multi-domain]  Cd Length: 80  Bit Score: 130.12  E-value: 3.51e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821324807  56 YRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRH 127
Cdd:cd18930    1 NRSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRF 72
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
 57-127 4.38e-36

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad family (Mad1, Mxi, Mad3, and Mad4) bear the bHLHzip domain (also known as basic-helix-loop-helix-leucine-zipper or bHLH-LZ domain), which mediates heterodimerization to Max and the sequence-specific DNA binding ability to E-box DNA. Mad family proteins can repress transcription at the E-box through their interaction with co-repressors. Mad family proteins antagonize Myc function in transactivation and transformation and they are growth/tumor suppressors. The developmental phenotypes of the individual Mad family member knockout mice are relatively mild- all these mice have been shown to be viable and normal.


Pssm-ID: 381407 [Multi-domain]  Cd Length: 76  Bit Score: 121.94  E-value: 4.38e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 821324807  57 RSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRH 127
Cdd:cd11401    1 RSTHNELEKNRRAHLRLCLERLKELVPLGPDATRHTTLSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQRE 71
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
 57-127 2.97e-30

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) and similar proteins; Mad1, also termed Max dimerization protein 1 (MXD1), or Max dimerizer 1, or protein MAD, is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX.


Pssm-ID: 381501 [Multi-domain]  Cd Length: 80  Bit Score: 107.01  E-value: 2.97e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 821324807  57 RSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRH 127
Cdd:cd18931    2 RSTHNEMEKNRRAHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRH 72
bHLHzip_Mad4 cd18929
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and ...
 55-127 9.24e-24

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and similar proteins; Mad4, also termed Max dimerization protein 4, or Max dimerizer 4 (MXD4), or Class C basic helix-loop-helix protein 12 (bHLHc12), or Max-interacting transcriptional repressor MAD4, is a bHLHZip Max-interacting transcriptional repressor that suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation. It is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc.


Pssm-ID: 381499 [Multi-domain]  Cd Length: 88  Bit Score: 90.45  E-value: 9.24e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821324807  55 HYRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRH 127
Cdd:cd18929    1 NNRSSHNELEKHRRAKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKMHIKKLEEQDRKALNIKEQLQREHRY 73
bHLHzip_Mad3 cd18932
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and ...
 57-126 4.93e-20

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and similar proteins; Mad3, also termed Max dimerization protein 3, or Max dimerizer 3 (MXD3), or Class C basic helix-loop-helix protein 13 (bHLHc13), or Max-interacting transcriptional repressor MAD3, or Myx, is a bHLHZip Max-interacting transcriptional repressor that plays an important role in cellular proliferation. It suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation.


Pssm-ID: 381502 [Multi-domain]  Cd Length: 85  Bit Score: 81.00  E-value: 4.93e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821324807  57 RSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQR 126
Cdd:cd18932    7 RSVHNELEKHRRAQLRRCLEQLKQQVPLGADCSRYTTLSLLRRARLHIQKLEEQEQRAQQLKERLRWEQQ 76
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
 57-127 2.77e-11

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar proteins; Mnt, also termed Class D basic helix-loop-helix protein 3 (bHLHd3), or Myc antagonist MNT, or protein ROX, is a bHLHZip transcriptional repressor that binds DNA as a heterodimer with MAX. It binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'. Mnt has an important role as an antagonist and regulator of Myc activities and it is a potential tumor suppressor. Mnt is ubiquitously expressed. Mnt-deficient mice shown to exhibit early postnatal lethality.


Pssm-ID: 381408 [Multi-domain]  Cd Length: 77  Bit Score: 57.33  E-value: 2.77e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 821324807  57 RSTHNELEKNRRAHLRLCLERLKTLIPlGPECSRHTTLGLLNKAKAHIKKLEeadRKSRYQLESLEREQRH 127
Cdd:cd11402    3 REVHNKLEKNRRAHLKECFETLKRQIP-NLDDKKTSNLNILRSALRYIQILK---RKEKEYEHEMERLARE 69
HLH pfam00010
Helix-loop-helix DNA-binding domain;
56-108 3.64e-11

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 56.31  E-value: 3.64e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 821324807   56 YRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLE 108
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
61-113 1.34e-10

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 54.92  E-value: 1.34e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 821324807    61 NELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRK 113
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
 57-126 7.34e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a member of the bHLHzip family of transcription factors that play important roles in the control of normal cell proliferation, growth, survival and differentiation. All Myc isoforms contain two independently functioning polypeptide chain regions: N-terminal transactivating residues and a C-terminal bHLHzip segment. The bHLHzip family of bHLH transcription factors are characterized by a highly conserved N-terminal basic region that may bind DNA at a consensus hexanucleotide sequence known as the E-box (CANNTG) followed by HLH and leucine zipper motifs that may interact with other proteins to form homo- and heterodimers. Myc heterodimerizes with Max enabling specific binding to E-box DNA sequences in the promoters of target genes. The Myc proto-oncoprotein family includes at least five different functional members: c-, N-, L-, S- and B-Myc (which is lacking the bHLH domain).


Pssm-ID: 381406 [Multi-domain]  Cd Length: 80  Bit Score: 45.62  E-value: 7.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821324807  57 RSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQR 126
Cdd:cd11400    2 RRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNE 71
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 64-109 1.83e-06

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 43.66  E-value: 1.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 821324807  64 EKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEE 109
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQS 46
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 57-123 3.76e-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: 37.66  E-value: 3.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 821324807  57 RSTHNELEKNRRAHLRLCLERLKTLIPlGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLER 123
Cdd:cd11404    3 RLNHVRSEKKRRELIKKGYDELCALVP-GLDPQKRTKADILQKAADWIQELKEENEKLEEQLDELKE 68
 
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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