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Conserved domains on  [gi|31322828|gb|AAP41731|]
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c-myc, partial [Casuarius casuarius]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
bHLHzip_c-Myc cd11458
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, ...
98-181 4.07e-44

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: 141.17  E-value: 4.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828  98 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHK 177
Cdd:cd11458   1 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQLRRRREQLKHR 80

                ....
gi 31322828 178 LEQL 181
Cdd:cd11458  81 LEQL 84
Myc_N super family cl03082
Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper ...
9-92 7.50e-42

Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper class of transcription factors, see pfam00010. Myc forms a heterodimer with Max, and this complex regulates cell growth through direct activation of genes involved in cell replication. Mutations in the C-terminal 20 residues of this domain cause unique changes in the induction of apoptosis, transformation, and G2 arrest.


The actual alignment was detected with superfamily member pfam01056:

Pssm-ID: 460045  Cd Length: 339  Bit Score: 143.39  E-value: 7.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828     9 IDVVTLAEANE-SESSTESSTETSEGHSKPHHSPLVLKRCHVNIHQHNYAAPPSTKVDYPAAKRLKLDS-GRVLKQISNN 86
Cdd:pfam01056 254 IDVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNN 333

                  ....*.
gi 31322828    87 RKCSSP 92
Cdd:pfam01056 334 RKCSSP 339
 
Name Accession Description Interval E-value
bHLHzip_c-Myc cd11458
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, ...
98-181 4.07e-44

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: 141.17  E-value: 4.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828  98 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHK 177
Cdd:cd11458   1 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQLRRRREQLKHR 80

                ....
gi 31322828 178 LEQL 181
Cdd:cd11458  81 LEQL 84
Myc_N pfam01056
Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper ...
9-92 7.50e-42

Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper class of transcription factors, see pfam00010. Myc forms a heterodimer with Max, and this complex regulates cell growth through direct activation of genes involved in cell replication. Mutations in the C-terminal 20 residues of this domain cause unique changes in the induction of apoptosis, transformation, and G2 arrest.


Pssm-ID: 460045  Cd Length: 339  Bit Score: 143.39  E-value: 7.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828     9 IDVVTLAEANE-SESSTESSTETSEGHSKPHHSPLVLKRCHVNIHQHNYAAPPSTKVDYPAAKRLKLDS-GRVLKQISNN 86
Cdd:pfam01056 254 IDVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNN 333

                  ....*.
gi 31322828    87 RKCSSP 92
Cdd:pfam01056 334 RKCSSP 339
HLH pfam00010
Helix-loop-helix DNA-binding domain;
102-154 4.96e-11

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 55.54  E-value: 4.96e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31322828   102 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQ 154
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
107-158 5.78e-11

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 55.30  E-value: 5.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 31322828    107 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEH 158
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQ 52
 
Name Accession Description Interval E-value
bHLHzip_c-Myc cd11458
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, ...
98-181 4.07e-44

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: 141.17  E-value: 4.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828  98 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHK 177
Cdd:cd11458   1 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQLRRRREQLKHR 80

                ....
gi 31322828 178 LEQL 181
Cdd:cd11458  81 LEQL 84
Myc_N pfam01056
Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper ...
9-92 7.50e-42

Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper class of transcription factors, see pfam00010. Myc forms a heterodimer with Max, and this complex regulates cell growth through direct activation of genes involved in cell replication. Mutations in the C-terminal 20 residues of this domain cause unique changes in the induction of apoptosis, transformation, and G2 arrest.


Pssm-ID: 460045  Cd Length: 339  Bit Score: 143.39  E-value: 7.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828     9 IDVVTLAEANE-SESSTESSTETSEGHSKPHHSPLVLKRCHVNIHQHNYAAPPSTKVDYPAAKRLKLDS-GRVLKQISNN 86
Cdd:pfam01056 254 IDVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNN 333

                  ....*.
gi 31322828    87 RKCSSP 92
Cdd:pfam01056 334 RKCSSP 339
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
102-181 5.32e-33

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: 112.64  E-value: 5.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd11400   1 KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRKKLERL 80
bHLHzip_N-Myc_like cd11456
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins; N-Myc, ...
98-182 8.31e-28

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins; N-Myc, also termed Class E basic helix-loop-helix protein 37 (bHLHe37), is a bHLHZip proto-oncogene protein that positively regulates the transcription of MYCNOS in neuroblastoma cells. It is also essential during embryonic development. N-Myc has a critical role in regulating the switch between proliferation and differentiation of progenitor cells. It binds DNA as a heterodimer with MAX. The family also includes S-Myc, encoded by rat or mouse intronless myc gene, which has apoptosis-inducing activity.


Pssm-ID: 381462 [Multi-domain]  Cd Length: 87  Bit Score: 99.98  E-value: 8.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828  98 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHK 177
Cdd:cd11456   1 EDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEQKLLLEKEKLQARQQQLLKK 80

                ....*
gi 31322828 178 LEQLR 182
Cdd:cd11456  81 IEQAR 85
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
96-184 5.69e-25

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, also termed Class E basic helix-loop-helix protein 38 (bHLHe38), or protein L-Myc-1, or V-myc myelocytomatosis viral oncogene homolog, is a bHLHZip oncoprotein belonging to the Myc oncogene protein family. It binds DNA as a heterodimer with MAX. L-Myc is co-expressed with another Myc family member and has weaker transformation/transactivation activities. L-Myc knockout mouse did not exhibit any phenotypic abnormalities.


Pssm-ID: 381463 [Multi-domain]  Cd Length: 89  Bit Score: 92.55  E-value: 5.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828  96 DSEENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLK 175
Cdd:cd11457   1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLL 80

                ....*....
gi 31322828 176 HKLEQLRNS 184
Cdd:cd11457  81 RRIAQLKGR 89
HLH pfam00010
Helix-loop-helix DNA-binding domain;
102-154 4.96e-11

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 55.54  E-value: 4.96e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31322828   102 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQ 154
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
107-158 5.78e-11

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 55.30  E-value: 5.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 31322828    107 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEH 158
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQ 52
bHLHzip_Max cd11406
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, ...
102-169 4.88e-10

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: 53.12  E-value: 4.88e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVAnNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRR 169
Cdd:cd11406   1 KRAHHNALERKRRDHIKDSFHSLRDSVPSLQ-GEKASRAQILKKATEYIQYMRRKNHTHQQDIDDLKR 67
Myc-LZ pfam02344
Myc leucine zipper domain; This family consists of the leucine zipper dimerization domain ...
155-181 1.30e-08

Myc leucine zipper domain; This family consists of the leucine zipper dimerization domain found in both cellular c-Myc proto-oncogenes and viral v-Myc oncogenes. dimerization via the leucine zipper motif with other basic helix-loop-helix-leucine zipper (b/HLH/lz) proteins such as Max is required for efficient DNA binding. The Myc-Max dimer is a transactivating complex activating expression of growth related genes promoting cell proliferation. The dimerization is facilitated via interdigitating leucine residues every 7th position of the alpha helix. Like charge repulsion of adjacent residues in this region perturbs the formation of homodimers with heterodimers being promoted by opposing charge attractions.


Pssm-ID: 460536  Cd Length: 27  Bit Score: 48.40  E-value: 1.30e-08
                          10        20
                  ....*....|....*....|....*..
gi 31322828   155 SDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:pfam02344   1 ADEQRLISEKDQLRKRREQLKHRLEQL 27
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
110-155 1.47e-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: 48.67  E-value: 1.47e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 31322828 110 ERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQS 155
Cdd:cd00083   1 ERRRRDKINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQS 46
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
103-178 2.49e-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: 48.75  E-value: 2.49e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKL 178
Cdd:cd11401   1 RSTHNELEKNRRAHLRLCLERLKELVPLGPDATRHTTLSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQRELKRRL 76
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
103-178 6.85e-07

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: 45.00  E-value: 6.85e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEvANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKL 178
Cdd:cd11402   3 REVHNKLEKNRRAHLKECFETLKRQIPN-LDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
103-168 2.99e-06

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: 43.03  E-value: 2.99e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEvANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd19682   1 RLRHKKRERERRSELRELFDKLKQLLGL-DSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARLT 65
bHLHzip_Mad4 cd18929
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and ...
103-181 3.42e-06

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: 43.46  E-value: 3.42e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd18929   3 RSSHNELEKHRRAKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKMHIKKLEEQDRKALNIKEQLQREHRYLKRRLEQL 81
bHLHzip_Mad3 cd18932
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and ...
103-181 2.24e-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: 41.32  E-value: 2.24e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd18932   7 RSVHNELEKHRRAQLRRCLEQLKQQVPLGADCSRYTTLSLLRRARLHIQKLEEQEQRAQQLKERLRWEQQKLRRRLESL 85
bHLH_TS cd11390
tissue specific basic helix-loop-helix (bHLH-TS) domain family; Tissue specific bHLH domain ...
103-154 3.58e-05

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: 39.86  E-value: 3.58e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQ 154
Cdd:cd11390   1 RNAANARERRRMHDLNDAFEALRKVLPTVPPDKKLSKIETLRLAINYIAALS 52
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
103-181 3.75e-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: 40.37  E-value: 3.75e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd18931   2 RSTHNEMEKNRRAHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80
bHLHzip_MGA cd18911
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and ...
103-168 5.27e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) 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.


Pssm-ID: 381481  Cd Length: 65  Bit Score: 39.77  E-value: 5.27e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIpEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd18911   1 RRTHTANERRRRNEMRDLFEKLKRTL-GLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
bHLHzip_SREBP_like cd11395
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
102-178 5.47e-05

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: 40.01  E-value: 5.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIP---------------EVANNEKAPKVVILKKATEYVLSIQSdehrliaEKEQ 166
Cdd:cd11395   3 KRLPHNAIEKRYRSNLNTKIERLRDAIPslrspegksddgglgGLAPTTKLSKATILTKAIEYIRHLEQ-------ENER 75
                        90
                ....*....|..
gi 31322828 167 LRRRREQLKHKL 178
Cdd:cd11395  76 LEEENEELRQQV 87
bHLHzip_MXI1 cd18930
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and ...
103-181 5.53e-05

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: 39.98  E-value: 5.53e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd18930   2 RSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRFLKRRLEQL 80
bHLH_AtFIT_like cd11450
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana Fe-deficiency induced ...
108-170 7.89e-05

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana Fe-deficiency induced transcription factor 1 (FIT) and similar proteins; The family includes bHLH transcription factors from Arabidopsis thaliana, such as FIT and DYT1. FIT, also termed FER-like iron deficiency-induced transcription factor, or FER-like regulator of iron uptake, or AtbHLH29, or EN 43, is a bHLH transcription factor that is required for the iron deficiency response in plant. It regulates FRO2 at the level of mRNA accumulation and IRT1 at the level of protein accumulation. DYT1, also termed AtbHLH22, or protein dysfunctional tapetum 1, or EN 49, is a bHLH transcription factor involved in the control of tapetum development. It is required for male fertility and pollen differentiation, especially during callose deposition.


Pssm-ID: 381456 [Multi-domain]  Cd Length: 76  Bit Score: 39.43  E-value: 7.89e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31322828 108 VLERQRRNELKLSFFALRDQIPEVANNEKAPkvvILKKATEYVLSIQSDEHRLIAEKEQLRRR 170
Cdd:cd11450   9 VSERNRRQKLNQRLFALRSVVPNITKMDKAS---IIKDAISYIQELQYQEKKLEAEIRELESR 68
bHLHzip_scHMS1_like cd11399
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae transcription ...
101-170 9.73e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae transcription factor HMS1 and similar proteins; HMS1, also termed high-copy MEP suppressor protein 1, is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation.


Pssm-ID: 381405 [Multi-domain]  Cd Length: 96  Bit Score: 39.76  E-value: 9.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828 101 DKRRTHNVLERQRRNELKLSFFALRDQIPE--------------------VANNEKAPKVVILKKATEYVLSIQSDEHRL 160
Cdd:cd11399   2 SKKTAHNMIEKRYRSNINDRIAELRDSVPAlreayksargededeedlggLTPATKLNKATILSKATEYIRHLEKKNKRL 81
                        90
                ....*....|
gi 31322828 161 IAEKEQLRRR 170
Cdd:cd11399  82 SRENASLRER 91
bHLHzip_spESC1_like cd19690
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) ...
103-168 1.06e-04

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: 38.98  E-value: 1.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31322828 103 RRTHNVLERQRRNELKLSFFALRDQIPEvANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd19690   1 RVSHKLAERKRRKEMKELFEDLRDALPQ-ERGTKASKWEILTKAISYIQQLKRHIRELRSEVNDLR 65
bHLHzip_scCBP1 cd11398
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae ...
102-182 1.96e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae centromere-binding protein 1 (CBP-1) and similar proteins; CBP-1, also termed centromere promoter factor 1 (CPF1), or centromere-binding factor 1 (CBF1), is a bHLHzip protein that is required for chromosome stability and methionine prototrophy. It binds as a homodimer to the centromere DNA elements I (CDEI, GTCACATG) region of the centromere that is required for optimal centromere function.


Pssm-ID: 381404 [Multi-domain]  Cd Length: 89  Bit Score: 38.86  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPevANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd11398   7 RRDNHKEVERRRRENINEGINELAALVP--GNAREKNKGAILARAVEYIQELQETEAKNIEKWTLEKLLTDQAIAELAAL 84

                .
gi 31322828 182 R 182
Cdd:cd11398  85 N 85
bHLHzip_SREBP2 cd18922
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
99-168 2.05e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 2 (SREBP2) and similar proteins; SREBP2, also termed Class D basic helix-loop-helix protein 2 (bHLHd2), or sterol regulatory element-binding transcription factor 2 (SREBF2), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcription activator of cholesterol biosynthesis.


Pssm-ID: 381492 [Multi-domain]  Cd Length: 77  Bit Score: 38.40  E-value: 2.05e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828  99 ENDKRRTHNVLERQRRNELKLSFFALRDQIpeVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd18922   3 EGERRTTHNIIEKRYRSSINDKIIELKDLV--MGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMALK 70
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
102-170 3.37e-04

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: 37.64  E-value: 3.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVAN--NEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRR 170
Cdd:cd11405   3 RRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQnpNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQLRQE 73
bHLH_TS_ATOH8 cd11421
basic helix-loop-helix (bHLH) domain found in protein atonal homolog 8 (ATOH8) and similar ...
101-153 6.64e-04

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: 36.64  E-value: 6.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 31322828 101 DKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSI 153
Cdd:cd11421   7 QRRIEANARERTRVHTISAAFEALRKAVPSYSYNQKLSKLAILRIACSYILAL 59
bHLH_TS_ASCL1_Mash1 cd19742
basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 1 (ASCL-1) and ...
107-166 6.84e-04

basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 1 (ASCL-1) and similar proteins; 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 a neural-specific bHLH transcription factor that 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.


Pssm-ID: 381585  Cd Length: 71  Bit Score: 36.66  E-value: 6.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31322828 107 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQS--DEHRLIAEKEQ 166
Cdd:cd19742  10 NERERNRVKLVNMGFATLREHVPNGAANKKMSKVETLRSAVEYIRALQQllDEHDAVSAAFQ 71
bHLH_TS_TWIST1 cd11412
basic helix-loop-helix (bHLH) domain found in twist-related protein 1 (TWIST1) and similar ...
90-157 1.44e-03

basic helix-loop-helix (bHLH) domain found in twist-related protein 1 (TWIST1) and similar proteins; TWIST1, also termed Class A basic helix-loop-helix protein 38 (bHLHa38), or H-twist, is a bHLH transcriptional regulator that inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. It also represses expression of proinflammatory cytokines such as TNFA and IL1B. In addition, TWIST1 is involved in cancer development and progression.


Pssm-ID: 381418 [Multi-domain]  Cd Length: 77  Bit Score: 35.92  E-value: 1.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31322828  90 SSPRTSDsEENDKRRTHNVLERQRRNELKLSFFALRDQIPEVAnNEKAPKVVILKKATEYV----LSIQSDE 157
Cdd:cd11412   1 GSPQSFE-ELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLP-SDKLSKIQTLKLAARYIdflyQVLQSDE 70
bHLH_TS_ASCL1_like cd19723
basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster achaete-scute complex ...
107-154 1.86e-03

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: 35.12  E-value: 1.86e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 31322828 107 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQ 154
Cdd:cd19723   6 NERERNRVKLVNLGFATLREHVPNGRANKKMSKVETLRSAVEYIRQLQ 53
bHLHzip_Mlx cd19687
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar ...
102-169 2.25e-03

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: 35.47  E-value: 2.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNE-----KAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRR 169
Cdd:cd19687   2 RREAHTQAEQKRRDAIKKGYDDLQDIVPTCQQQDdigsqKLSKATILQRSIDYIQFLHQQKKKQEEELSALRK 74
bHLH_AtAIB_like cd11449
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein ABA-INDUCIBLE ...
110-175 2.42e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein ABA-INDUCIBLE bHLH-TYPE (AIB) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as AIB and MYC proteins (MYC2, MYC3 and MYC4). AIB, also termed AtbHLH17, or EN 35, is a transcription activator that regulates positively abscisic acid (ABA) response. MYC2, also termed protein jasmonate insensitive 1, or R-homologous Arabidopsis protein 1 (RAP-1), or AtbHLH6, or EN 38, or Z-box binding factor 1 protein, is a transcriptional activator involved in abscisic acid (ABA), jasmonic acid (JA), and light signaling pathways. MYC3, also termed protein altered tryptophan regulation 2, or AtbHLH5, or transcription factor ATR2, or EN 36, is a transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. MYC4, also termed AtbHLH4, or EN 37, is a transcription factor involved in jasmonic acid (JA) gene regulation. MYC2, together with MYC3 and MYC4, controls additively subsets of JA-dependent responses.


Pssm-ID: 381455 [Multi-domain]  Cd Length: 78  Bit Score: 35.44  E-value: 2.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31322828 110 ERQRRNELKLSFFALRDQIPEVANNEKAPkvvILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLK 175
Cdd:cd11449  13 ERQRREKLNQRFYALRAVVPNVSKMDKAS---LLGDAISYINELKSKVQDMETEKKEMKRQESEKK 75
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
102-171 2.64e-03

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: 34.97  E-value: 2.64e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVaNNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRR 171
Cdd:cd11404   2 RRLNHVRSEKKRRELIKKGYDELCALVPGL-DPQKRTKADILQKAADWIQELKEENEKLEEQLDELKEAA 70
bHLH_TS_ASCL2_Mash2 cd19743
basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 2 (ASCL-2) and ...
107-155 2.90e-03

basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 2 (ASCL-2) and similar proteins; 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 a bHLH transcription factor that is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves.


Pssm-ID: 381586  Cd Length: 64  Bit Score: 34.94  E-value: 2.90e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 31322828 107 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQS 155
Cdd:cd19743   8 NERERNRVKLVNLGFAALRQHVPQGGASKKMSKVETLRSAVEYIRALQR 56
bHLH_AtMYC1_like cd18918
basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; ...
106-182 3.38e-03

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: 35.00  E-value: 3.38e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31322828 106 HNVLERQRRNELKLSFFALRDQIPEVANNEKAPkvvILKKATEYVlsiqsdehrliaekEQLRRRREQLKHKLEQLR 182
Cdd:cd18918   1 LFATERERREKLNEKFSDLRNLIPNPTKNDRAS---ILSDAIKYI--------------NELQRTVEELKSLVEKKR 60
bHLH_TS_MIST1 cd19711
basic helix-loop-helix (bHLH) domain found in muscle, intestine and stomach expression 1 ...
102-155 6.12e-03

basic helix-loop-helix (bHLH) domain found in muscle, intestine and stomach expression 1 (MIST-1) and similar proteins; MIST-1, also termed Class A basic helix-loop-helix protein 15 (bHLHa15), or Class B basic helix-loop-helix protein 8 (bHLHb8), is a bHLH transcription factor expressed in pancreatic acinar cells and other serous exocrine cells. It is essential for cytoskeletal organization and secretory activity. It also functions as a potent endoplasmic reticulum (ER) stress-inducible transcriptional regulator. MIST-1 is capable of binding to E-box (CANNTG) motifs as a homodimer or a heterodimer with E-proteins (E12 and E47) to regulate transcription.


Pssm-ID: 381554  Cd Length: 62  Bit Score: 33.92  E-value: 6.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQS 155
Cdd:cd19711   1 RRLESNERERQRMHKLNNAFQALREVIPHVRAEKKLSKIETLTLAKNYIKSLTT 54
bHLH_AtORG2_like cd18914
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana OBP3-responsive gene 2 ...
102-170 6.20e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana OBP3-responsive gene 2 (ORG2), 3 (ORG3) and similar proteins; The family includes ORG2 (also termed AtbHLH38, or EN 8) and ORG3 (also termed AtbHLH39, or EN 9), both of which act as bHLH transcription factors.


Pssm-ID: 381484 [Multi-domain]  Cd Length: 77  Bit Score: 34.20  E-value: 6.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRR 170
Cdd:cd18914   1 KKLLHNDVERQRRQEMASLFSSLRSLLPLQYIKGKLSVSDHVDEAVNYIKELQEKIKELSEKRDELLKL 69
bHLHzip_SREBP1 cd18921
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
101-168 8.16e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 1 (SREBP1) and similar proteins; SREBP1, also termed Class D basic helix-loop-helix protein 1 (bHLHd1), or sterol regulatory element-binding transcription factor 1 (SREBF1), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcriptional activator required for lipid homeostasis. It may control transcription of the low-density lipoprotein receptor gene as well as the fatty acid. SREBP1 has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3').


Pssm-ID: 381491  Cd Length: 75  Bit Score: 34.10  E-value: 8.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31322828 101 DKRRTHNVLERQRRNELKLSFFALRDQIpeVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd18921   5 EKRTAHNAIEKRYRSSINDKIIELKDLV--VGTEAKLNKSAVLRKAIDYIRFLQQSNQKLKQENMALK 70
bHLH_TS_scleraxis cd18951
basic helix-loop-helix (bHLH) domain found in scleraxis and similar proteins; Scleraxis, also ...
99-150 8.75e-03

basic helix-loop-helix (bHLH) domain found in scleraxis and similar proteins; Scleraxis, also termed SCX, or Class A basic helix-loop-helix protein 41 (bHLHa41), or Class A basic helix-loop-helix protein 48 (bHLHa48), is a bHLH transcription factor that is expressed in sclerotome limb bud cranial and body wall mesenchyme, pericardium and heart valves, ligaments and tendons. It is required for tendon formation ligaments, connective tissue, the diaphragm, and testis development. Scleraxis plays a central role in promoting fibroblast proliferation and matrix synthesis during the embryonic development of tendons.


Pssm-ID: 381521 [Multi-domain]  Cd Length: 68  Bit Score: 33.59  E-value: 8.75e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 31322828  99 ENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYV 150
Cdd:cd18951   1 EPRQRHTANARERDRTNSVNTAFTALRTLIPTEPADRKLSKIETLRLASSYI 52
bHLH_TS_taxi_Dei cd11431
basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein taxi and similar ...
102-150 9.13e-03

basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster protein taxi and similar proteins; Protein taxi, also termed protein delilah (Dei), is a bHLH transcription factor that is involved in regulation of cell adhesion and attachment that is expressed in specialized cells that provide anchoring sites to either muscles (tendon cells), or proprioceptors (chordotonal attachment cells) during embryonic development. It probably plays an important role in the differentiation of epidermal cells into the tendon cells that form the attachment sites for all muscles.


Pssm-ID: 381437 [Multi-domain]  Cd Length: 59  Bit Score: 33.17  E-value: 9.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIPEV---ANNEKAPKVVILKKATEYV 150
Cdd:cd11431   1 RRKTANARERDRMREINDAFEALRRAVPEYpvaGKDGKLTKITTLRLAMNYI 52
bHLHzip_SREBP cd11394
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
102-171 9.62e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family; 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.


Pssm-ID: 381400 [Multi-domain]  Cd Length: 73  Bit Score: 33.79  E-value: 9.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31322828 102 KRRTHNVLERQRRNELKLSFFALRDQIpeVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRR 171
Cdd:cd11394   6 KRSAHNAIEKRYRSSINDRIIELKDLV--VGPDAKMNKSAVLRKAIDYIRYLQKVNQKLKQENMALKKAL 73
 
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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