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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353329028    1 DVVTLAEANE-SESSTESSTETSEEHSKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLRLDS-GRVLKQISNNR 78
Cdd:pfam01056 255 DVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNNR 334

                  ....*
gi 353329028   79 KCSSP 83
Cdd:pfam01056 335 KCSSP 339

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353329028    1 DVVTLAEANE-SESSTESSTETSEEHSKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLRLDS-GRVLKQISNNR 78
Cdd:pfam01056 255 DVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNNR 334

                  ....*
gi 353329028   79 KCSSP 83
Cdd:pfam01056 335 KCSSP 339

Helix-loop-helix DNA-binding domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 353329028   93 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQ 145
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353329028    1 DVVTLAEANE-SESSTESSTETSEEHSKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLRLDS-GRVLKQISNNR 78
Cdd:pfam01056 255 DVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNNR 334

                  ....*
gi 353329028   79 KCSSP 83
Cdd:pfam01056 335 KCSSP 339

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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353329028  93 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRREQLK 166
Cdd:cd11400    1 KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLR 74

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353329028  87 DSEENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRREQL 165
Cdd:cd11457    1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQL 79

helix loop helix domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 353329028    98 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQADEH 149
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQ 52

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 353329028 101 ERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQA 146
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQS 46

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353329028  94 RRTHNVLERQRRNELKLSFFALRDQIPEvANNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRREQL 165
Cdd:cd11402    3 REVHNKLEKNRRAHLKECFETLKRQIPN-LDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIAL 73

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 353329028  94 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQ 145
Cdd:cd11390    1 RNAANARERRRMHDLNDAFEALRKVLPTVPPDKKLSKIETLRLAINYIAALS 52

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.

                          10        20
                  ....*....|....*....|.
gi 353329028  146 ADEHRLIAEKEQLRRRREQLK 166
Cdd:pfam02344   1 ADEQRLISEKDQLRKRREQLK 21

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353329028  92 DKRRTHNVLERQRRNELKLSFFALRDQIPE--------------------VANNEKAPKVVILKKATEYVLSIQADEHRL 151
Cdd:cd11399    2 SKKTAHNMIEKRYRSNINDRIAELRDSVPAlreayksargededeedlggLTPATKLNKATILSKATEYIRHLEKKNKRL 81

                         90
                 ....*....|
gi 353329028 152 IAEKEQLRRR 161
Cdd:cd11399   82 SRENASLRER 91

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353329028  99 VLERQRRNELKLSFFALRDQIPEVANNEKAPkvvILKKATEYVLSIQADEHRLIAEKEQLRRR 161
Cdd:cd11450    9 VSERNRRQKLNQRLFALRSVVPNITKMDKAS---IIKDAISYIQELQYQEKKLEAEIRELESR 68

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'.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353329028  93 KRRTHNVLERQRRNELKLSFFALRDQIPEVAN--NEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRR 161
Cdd:cd11405    3 RRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQnpNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQLRQE 73

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353329028  93 KRRTHNVLERQRRNELKLSFFALRDQIPEVaNNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRR 162
Cdd:cd11404    2 RRLNHVRSEKKRRELIKKGYDELCALVPGL-DPQKRTKADILQKAADWIQELKEENEKLEEQLDELKEAA 70

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353329028  94 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRREQLK 166
Cdd:cd18929    3 RSSHNELEKHRRAKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKMHIKKLEEQDRKALNIKEQLQREHRYLK 75

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353329028  93 KRRTHNVLERQRRNELKLSFFALRDQIPevANNEKAPKVVILKKATEYVLSIQADEHRLI-------AEKEQLRRRREQL 165
Cdd:cd11398    7 RRDNHKEVERRRRENINEGINELAALVP--GNAREKNKGAILARAVEYIQELQETEAKNIekwtlekLLTDQAIAELAAL 84

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 353329028  98 NVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQA 146
Cdd:cd19743    8 NERERNRVKLVNLGFAALRQHVPQGGASKKMSKVETLRSAVEYIRALQR 56

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353329028  94 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRREQLK 166
Cdd:cd18932    7 RSVHNELEKHRRAQLRRCLEQLKQQVPLGADCSRYTTLSLLRRARLHIQKLEEQEQRAQQLKERLRWEQQKLR 79

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353329028  93 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNE-----KAPKVVILKKATEYVLSIQADEHRLIAEKEQLRR 160
Cdd:cd19687    2 RREAHTQAEQKRRDAIKKGYDDLQDIVPTCQQQDdigsqKLSKATILQRSIDYIQFLHQQKKKQEEELSALRK 74

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 353329028  93 KRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQA 146
Cdd:cd19711    1 RRLESNERERQRMHKLNNAFQALREVIPHVRAEKKLSKIETLTLAKNYIKSLTT 54

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353329028  94 RRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQADEHRLIAEKEQLRRRREQLK 166
Cdd:cd18931    2 RSTHNEMEKNRRAHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLK 74

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 353329028  90 ENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYV 141
Cdd:cd18951    1 EPRQRHTANARERDRTNSVNTAFTALRTLIPTEPADRKLSKIETLRLASSYI 52