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Conserved domains on  [gi|568972021|ref|XP_006532465|]
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max-binding protein MNT isoform X1 [Mus musculus]

Protein Classification

basic helix-loop-helix domain-containing protein( domain architecture ID 14413204)

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
SCOP:  4000913

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
221-284 1.64e-37

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: 133.21  E-value: 1.64e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 221 RAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRL 284
Cdd:cd11402   14 RAHLKECFETLKRQIPNLDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77
 
Name Accession Description Interval E-value
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
221-284 1.64e-37

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: 133.21  E-value: 1.64e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 221 RAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRL 284
Cdd:cd11402   14 RAHLKECFETLKRQIPNLDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77
HLH smart00353
helix loop helix domain;
215-265 1.19e-08

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 51.07  E-value: 1.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568972021   215 KKRpggRAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKE 265
Cdd:smart00353   5 RRR---RRKINEAFDELRSLLPtLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
HLH pfam00010
Helix-loop-helix DNA-binding domain;
215-260 1.44e-07

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 48.22  E-value: 1.44e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568972021  215 KKRpggRAHLKECFETLKRNIPNV-DDKKTSNLSVLRTALRYIQSLK 260
Cdd:pfam00010  10 RRR---RDRINDAFDELRELLPTLpPDKKLSKAEILRLAIEYIKHLQ 53
 
Name Accession Description Interval E-value
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
221-284 1.64e-37

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: 133.21  E-value: 1.64e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 221 RAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRL 284
Cdd:cd11402   14 RAHLKECFETLKRQIPNLDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
215-287 1.04e-13

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: 66.42  E-value: 1.04e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 215 KKRpggRAHLKECFETLKRNIPNVDDK-KTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAEL 287
Cdd:cd11400   10 RQR---RNDLKNSFEKLRDLVPELADNeKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRKKLERL 80
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
215-261 1.04e-08

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: 51.37  E-value: 1.04e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568972021 215 KKRpggRAHLKECFETLKRNIPNV-DDKKTSNLSVLRTALRYIQSLKR 261
Cdd:cd00083    2 RRR---RDKINDAFEELKRLLPELpDSKKLSKASILQKAVEYIRELQS 46
HLH smart00353
helix loop helix domain;
215-265 1.19e-08

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 51.07  E-value: 1.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568972021   215 KKRpggRAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKE 265
Cdd:smart00353   5 RRR---RRKINEAFDELRSLLPtLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
215-284 1.61e-08

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: 51.44  E-value: 1.61e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568972021 215 KKRpggRAHLKECFETLKRNIPNVDD--KKTSnLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRL 284
Cdd:cd11401    9 KNR---RAHLRLCLERLKELVPLGPDatRHTT-LSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQRELKRRL 76
bHLHzip_Max cd11406
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, ...
214-276 2.46e-08

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, also termed Class D basic helix-loop-helix protein 4 (bHLHd4), or Myc-associated factor X, is a bHLHZip transcription regulator that forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a transcriptional repressor. Max homodimer bind DNA but is transcriptionally inactive. Targeted deletion of max results in early embryonic lethality in mice.


Pssm-ID: 381412  Cd Length: 69  Bit Score: 50.81  E-value: 2.46e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972021 214 QKKRpggRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLARE 276
Cdd:cd11406    9 ERKR---RDHIKDSFHSLRDSVPSLQGEKASRAQILKKATEYIQYMRRKNHTHQQDIDDLKRQ 68
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
210-273 8.78e-08

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: 49.19  E-value: 8.78e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 210 KSSEqKKRpggRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERL 273
Cdd:cd19682    5 KKRE-RER---RSELRELFDKLKQLLGLDSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARL 64
HLH pfam00010
Helix-loop-helix DNA-binding domain;
215-260 1.44e-07

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 48.22  E-value: 1.44e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568972021  215 KKRpggRAHLKECFETLKRNIPNV-DDKKTSNLSVLRTALRYIQSLK 260
Cdd:pfam00010  10 RRR---RDRINDAFDELRELLPTLpPDKKLSKAEILRLAIEYIKHLQ 53
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
211-276 1.09e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), MLX-interacting protein-like (MLXIPL) and similar proteins; The family includes MLXIP and MLXIPL. 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. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.


Pssm-ID: 381411 [Multi-domain]  Cd Length: 74  Bit Score: 46.50  E-value: 1.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568972021 211 SSEQKKRpggrAHLKECFETLKRNIPN---VDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLARE 276
Cdd:cd11405    9 SAEQKRR----FNIKSGFDTLQSLIPSlgqNPNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQLRQE 73
bHLHzip_MXI1 cd18930
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and ...
221-287 1.64e-06

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: 46.14  E-value: 1.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568972021 221 RAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAEL 287
Cdd:cd18930   13 RAHLRLCLERLKVLIPlGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRFLKRRLEQL 80
bHLH_AtMYC1_like cd18918
basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; ...
213-272 3.23e-06

basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; MYC1, also termed AtbHLH12, or EN 58, acts as a transcription activator, when associated with MYB75/PAP1 or MYB90/PAP2.


Pssm-ID: 381488 [Multi-domain]  Cd Length: 70  Bit Score: 45.02  E-value: 3.23e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972021 213 EQKKRpggRAHLKECFETLKRNIPNVDdkKTSNLSVLRTALRYIQSLKRKEKEYEHEMER 272
Cdd:cd18918    4 TERER---REKLNEKFSDLRNLIPNPT--KNDRASILSDAIKYINELQRTVEELKSLVEK 58
bHLHzip_Mad3 cd18932
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and ...
221-287 1.55e-05

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: 43.64  E-value: 1.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568972021 221 RAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAEL 287
Cdd:cd18932   18 RAQLRRCLEQLKQQVPlGADCSRYTTLSLLRRARLHIQKLEEQEQRAQQLKERLRWEQQKLRRRLESL 85
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
209-287 1.58e-05

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: 43.45  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972021 209 AKSSEQKKRPGGRAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAEL 287
Cdd:cd18931    1 SRSTHNEMEKNRRAHLRLCLEKLKMLVPlGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80
bHLHzip_MLXIP cd19688
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and ...
211-278 1.31e-04

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: 40.32  E-value: 1.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568972021 211 SSEQKKRpggrAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLaREKI 278
Cdd:cd19688    9 SAEQKRR----FNIKICFDTLNSLVStLKNSKPISNAITLQKTVEYIAKLQQERTQMQEETKRL-REEI 72
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
204-293 2.87e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 42.64  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972021 204 APAEEAKSSEQ---KKRPGGRAH---LKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKE----YEHEMERL 273
Cdd:cd07671   32 AQAEERYGKELvqiARKAGGQTEintLKASFDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEqrkkYEAVMERV 111
                         90       100
                 ....*....|....*....|
gi 568972021 274 AREKIATQQRLAELKHELSQ 293
Cdd:cd07671  112 QKSKVSLYKKTMESKKTYEQ 131
bHLH_TS_ASCL1_like cd19723
basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster achaete-scute complex ...
217-261 9.66e-04

basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster achaete-scute complex (AS-C) proteins, achaete-scute-like proteins, ASCL1-2, and similar proteins; This subfamily includes Drosophila melanogaster AS-C proteins and two ASCL family of transcription factors, ASCL-1 and ASCL-2. Drosophila melanogaster AS-C proteins includes lethal of scute (also known as achaete-scute complex protein T3 or AST3), scute (also known as achaete-scute complex protein T4 or AST4), achaete (also known as achaete-scute complex protein T5 or AST5), and asense (also known as achaete-scute complex protein T8 or AST8). They are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system, as well as in sex determination and dosage compensation. ASCL-1, also termed Class A basic helix-loop-helix protein 46 (bHLHa46), or achaete-scute homolog 1 (ASH-1), or mammalian achaete scute homolog 1 (Mash1), is expressed in subsets of neural progenitors in both the central and peripheral nervous system. It plays a key role in neuronal differentiation and specification in the nervous system. ASCL-2, also termed achaete-scute homolog 2 (ASH-2), or Class A basic helix-loop-helix protein 45 (bHLHa45), or mammalian achaete scute homolog 2 (Mash2), is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves.


Pssm-ID: 381566  Cd Length: 56  Bit Score: 37.43  E-value: 9.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568972021 217 RPGGRAHL-KECFETLKRNIPN-VDDKKTSNLSVLRTALRYIQSLKR 261
Cdd:cd19723    8 RERNRVKLvNLGFATLREHVPNgRANKKMSKVETLRSAVEYIRQLQQ 54
bHLH_TS cd11390
tissue specific basic helix-loop-helix (bHLH-TS) domain family; Tissue specific bHLH domain ...
221-261 1.15e-03

tissue specific basic helix-loop-helix (bHLH-TS) domain family; Tissue specific bHLH domain family includes transcription regulators whose expression are restricted to certain tissues. They are involved in cell-fate determination and process in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis and include proteins from myogenic regulatory factor (MRF) family, twist-related protein (TWIST) family, scleraxis-like family, heart- and neural crest derivatives-expressed protein (HAND) family, helix-loop-helix protein (HEN) family, musculin-like family, germline alpha (FIGLA) family, T-cell acute lymphocytic leukemia protein/ lymphoblastic leukemia-derived sequence (TAL/LYL) family, ovary, uterus and testis protein (OUT) family, mesoderm posterior protein (Mesp) family, muscle, intestine and stomach expression 1 (MIST-1) family, protein atonal homologs (ATOH) family, neurogenin (NGN) family, neurogenic differentiation factor (NeuroD) family, achaete-scute complex-like (ASCL) family, Fer3-like protein (FERD3L)-like family, and Oligodendrocyte lineage genes (OLIG) family of transcription factors.


Pssm-ID: 381396 [Multi-domain]  Cd Length: 55  Bit Score: 37.17  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568972021 221 RAH-LKECFETLKRNIPNV-DDKKTSNLSVLRTALRYIQSLKR 261
Cdd:cd11390   11 RMHdLNDAFEALRKVLPTVpPDKKLSKIETLRLAINYIAALSD 53
bHLHzip_Mad4 cd18929
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and ...
210-287 1.33e-03

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: 38.06  E-value: 1.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568972021 210 KSSEQKKRPGGRAHLKECFETLKRNIP-NVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAEL 287
Cdd:cd18929    3 RSSHNELEKHRRAKLRLYLEQLKQLVPlGPDSTRHTTLSLLKRAKMHIKKLEEQDRKALNIKEQLQREHRYLKRRLEQL 81
bHLHzip_c-Myc cd11458
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, ...
221-293 3.21e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, also termed Myc proto-oncogene protein, or Class E basic helix-loop-helix protein 39 (bHLHe39), or transcription factor p64, a bHLHZip proto-oncogene protein that functions as a transcription factor, which binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. It activates the transcription of growth-related genes.


Pssm-ID: 381464 [Multi-domain]  Cd Length: 84  Bit Score: 36.78  E-value: 3.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 221 RAHLKECFETLKRNIPNV-DDKKTSNLSVLRTALRYIQSLKRKEKeyehemeRLAREKIATQQRLAELKHELSQ 293
Cdd:cd11458   17 RNELKLSFFALRDQIPEVaNNEKAPKVVILKKATEYILSMQADEQ-------RLISEKEQLRRRREQLKHRLEQ 83
bHLH_TS_ATOH8 cd11421
basic helix-loop-helix (bHLH) domain found in protein atonal homolog 8 (ATOH8) and similar ...
221-261 3.72e-03

basic helix-loop-helix (bHLH) domain found in protein atonal homolog 8 (ATOH8) and similar proteins; ATOH8, also termed Class A basic helix-loop-helix protein 21 (bHLHa21), or helix-loop-helix protein hATH-6 (hATH6), is a bHLH shear-stress-responsive transcription factor expressed in activated satellite cells and proliferating myoblasts of human skeletal muscle tissue. It regulates endothelial cell proliferation, migration and tube-like structures formation. ATOH8 binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins.


Pssm-ID: 381427 [Multi-domain]  Cd Length: 68  Bit Score: 36.26  E-value: 3.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568972021 221 RAH-LKECFETLKRNIPN-VDDKKTSNLSVLRTALRYIQSLKR 261
Cdd:cd11421   19 RVHtISAAFEALRKAVPSySYNQKLSKLAILRIACSYILALAR 61
bHLHzip_spESC1_like cd19690
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) ...
210-273 5.13e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins; 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: 381533  Cd Length: 65  Bit Score: 35.90  E-value: 5.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972021 210 KSSEQKKRpggrAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERL 273
Cdd:cd19690    5 KLAERKRR----KEMKELFEDLRDALPQERGTKASKWEILTKAISYIQQLKRHIRELRSEVNDL 64
bHLHzip_SREBP_like cd11395
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
221-276 8.53e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family and similar proteins; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box. The family also includes Saccharomyces cerevisiae transcription factor HMS1 (also termed high-copy MEP suppressor protein 1) and serine-rich protein TYE7. HMS1 is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation. TYE7, also termed basic-helix-loop-helix protein SGC1, is a putative bHLHzip transcription activator required for Ty1-mediated glycolytic gene expression. TYE7 N-terminal is extremely rich in serine residues. It binds DNA on E-box motifs, 5'-CANNTG-3'. TYE7 is not essential for growth.


Pssm-ID: 381401 [Multi-domain]  Cd Length: 87  Bit Score: 35.77  E-value: 8.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568972021 221 RAHLKECFETLKRNIP--NVDDKKTSNL--------------SVLRTALRYIQSLKRKEKEYEHEMERLARE 276
Cdd:cd11395   15 RSNLNTKIERLRDAIPslRSPEGKSDDGglgglapttklskaTILTKAIEYIRHLEQENERLEEENEELRQQ 86
 
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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