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 153946419   13 PVSASLACKNYDYDYDSIQPYFYfdNDDEDFYHhqqGQTQPSAPSEDIWKKFELLPTPPLSPSRRQSL-----STAEQLE 87
Cdd:pfam01056   1 PLNSGMISKNYDLDYDSLQPCFY--PEEEDFYF---SGLQPPAPSEDIWKKFELLPTPPLSPSRRSSLsspfpSTADQLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419   88 MVSEFLGDDVVSQSFICDdADYSQSFIKSIIIQDCMWSGFSAAAKLEKVVSERLASLHAERKELMS-------------- 153
Cdd:pfam01056  76 MVTELLGADLVNQSFICD-PDEDDSFLKSIIIQDCMWSGFSAAAKLEKVVSEKLASGQAARKEGAAtlaagaassagrah 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419  154 --DSNSNRLNASYLQDLSTSASECIDPSVVFPYPLTECGKAGKVASPQPMLVLDTPPNSSSSSGSDSEDEEEEDEEEEEE 231
Cdd:pfam01056 155 sgSAGGGRSSSGYLQDLSHSASECVDPSVVFPFPLNKREKAPVPPAPSPALALDPPATPPRSSGSSSSSGDSKGLSSSGE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419  232 EEEEEEEEEEEE-------IDVVTVEKRQ---KRHE-----TDASESR-YPSPLVLKRCHVSTHQHNYAAHPSTRHDQPA 295
Cdd:pfam01056 235 DTLSDSDDEEEEeeeeeeeIDVVTVEKRQpssKRKEvstltTALGHSRpQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPP 314

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 153946419  296 VKRLRLEAsnnhsinsssSNRHVKQ----RKCASP 326
Cdd:pfam01056 315 QKRLKLES----------SGRVLKQisnnRKCSSP 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 153946419   13 PVSASLACKNYDYDYDSIQPYFYfdNDDEDFYHhqqGQTQPSAPSEDIWKKFELLPTPPLSPSRRQSL-----STAEQLE 87
Cdd:pfam01056   1 PLNSGMISKNYDLDYDSLQPCFY--PEEEDFYF---SGLQPPAPSEDIWKKFELLPTPPLSPSRRSSLsspfpSTADQLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419   88 MVSEFLGDDVVSQSFICDdADYSQSFIKSIIIQDCMWSGFSAAAKLEKVVSERLASLHAERKELMS-------------- 153
Cdd:pfam01056  76 MVTELLGADLVNQSFICD-PDEDDSFLKSIIIQDCMWSGFSAAAKLEKVVSEKLASGQAARKEGAAtlaagaassagrah 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419  154 --DSNSNRLNASYLQDLSTSASECIDPSVVFPYPLTECGKAGKVASPQPMLVLDTPPNSSSSSGSDSEDEEEEDEEEEEE 231
Cdd:pfam01056 155 sgSAGGGRSSSGYLQDLSHSASECVDPSVVFPFPLNKREKAPVPPAPSPALALDPPATPPRSSGSSSSSGDSKGLSSSGE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419  232 EEEEEEEEEEEE-------IDVVTVEKRQ---KRHE-----TDASESR-YPSPLVLKRCHVSTHQHNYAAHPSTRHDQPA 295
Cdd:pfam01056 235 DTLSDSDDEEEEeeeeeeeIDVVTVEKRQpssKRKEvstltTALGHSRpQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPP 314

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 153946419  296 VKRLRLEAsnnhsinsssSNRHVKQ----RKCASP 326
Cdd:pfam01056 315 QKRLKLES----------SGRVLKQisnnRKCSSP 339

helix loop helix domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 153946419   341 NVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQLDEQ 392
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQ 52

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 153946419   13 PVSASLACKNYDYDYDSIQPYFYfdNDDEDFYHhqqGQTQPSAPSEDIWKKFELLPTPPLSPSRRQSL-----STAEQLE 87
Cdd:pfam01056   1 PLNSGMISKNYDLDYDSLQPCFY--PEEEDFYF---SGLQPPAPSEDIWKKFELLPTPPLSPSRRSSLsspfpSTADQLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419   88 MVSEFLGDDVVSQSFICDdADYSQSFIKSIIIQDCMWSGFSAAAKLEKVVSERLASLHAERKELMS-------------- 153
Cdd:pfam01056  76 MVTELLGADLVNQSFICD-PDEDDSFLKSIIIQDCMWSGFSAAAKLEKVVSEKLASGQAARKEGAAtlaagaassagrah 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419  154 --DSNSNRLNASYLQDLSTSASECIDPSVVFPYPLTECGKAGKVASPQPMLVLDTPPNSSSSSGSDSEDEEEEDEEEEEE 231
Cdd:pfam01056 155 sgSAGGGRSSSGYLQDLSHSASECVDPSVVFPFPLNKREKAPVPPAPSPALALDPPATPPRSSGSSSSSGDSKGLSSSGE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419  232 EEEEEEEEEEEE-------IDVVTVEKRQ---KRHE-----TDASESR-YPSPLVLKRCHVSTHQHNYAAHPSTRHDQPA 295
Cdd:pfam01056 235 DTLSDSDDEEEEeeeeeeeIDVVTVEKRQpssKRKEvstltTALGHSRpQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPP 314

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 153946419  296 VKRLRLEAsnnhsinsssSNRHVKQ----RKCASP 326
Cdd:pfam01056 315 QKRLKLES----------SGRVLKQisnnRKCSSP 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419 336 KRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQLDEQRLLSIKEQLRRKSEQLKHRLQQL 415
Cdd:cd11400    1 KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRKKLERL 80

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419 330 DSEDNDKRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQLDEQRLLSIKEQLRRKSEQLK 409
Cdd:cd11457    1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLL 80

                 ....*....
gi 153946419 410 HRLQQLRSS 418
Cdd:cd11457   81 RRIAQLKGR 89

helix loop helix domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 153946419   341 NVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQLDEQ 392
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQ 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 153946419  390 DEQRLLSIKEQLRRKSEQLKHRLQQL 415
Cdd:pfam02344   2 DEQRLISEKDQLRKRREQLKHRLEQL 27

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 153946419 344 ERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQ 388
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQ 45

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153946419 337 RRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQLDEQRLLSIKEQLRRKSEQLKHRL 412
Cdd:cd11401    1 RSTHNELEKNRRAHLRLCLERLKELVPLGPDATRHTTLSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQRELKRRL 76

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 153946419 337 RRTHNVLERQRRNELKLSFFALRDEIPEvANNEKAAKVVILKKATECIHSMQLDEQRLLSIKEQLRRKSEQLKHRL 412
Cdd:cd11402    3 REVHNKLEKNRRAHLKECFETLKRQIPN-LDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153946419 336 KRRTHNVLERQRRNELKLSFFALRDEIP---------------EVANNEKAAKVVILKKATECIHSMQLDEQRL 394
Cdd:cd11395    3 KRLPHNAIEKRYRSNLNTKIERLRDAIPslrspegksddgglgGLAPTTKLSKATILTKAIEYIRHLEQENERL 76

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 153946419 336 KRRTHNVLERQRRNELKLSFFALRDEIPevANNEKAAKVVILKKATECIHSMQLDEQRLLSIKEQLRRKSEQLKHRLQQL 415
Cdd:cd11398    7 RRDNHKEVERRRRENINEGINELAALVP--GNAREKNKGAILARAVEYIQELQETEAKNIEKWTLEKLLTDQAIAELAAL 84

                 .
gi 153946419 416 R 416
Cdd:cd11398   85 N 85

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 153946419 337 RRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQ 388
Cdd:cd11390    1 RNAANARERRRMHDLNDAFEALRKVLPTVPPDKKLSKIETLRLAINYIAALS 52

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 153946419 335 DKRRTHNVLERQRRNELKLSFFALRDEIPE--------------------VANNEKAAKVVILKKATECIHSMQLDEQrl 394
Cdd:cd11399    2 SKKTAHNMIEKRYRSNINDRIAELRDSVPAlreayksargededeedlggLTPATKLNKATILSKATEYIRHLEKKNK-- 79

                         90
                 ....*....|....*...
gi 153946419 395 lsikeQLRRKSEQLKHRL 412
Cdd:cd11399   80 -----RLSRENASLRERL 92

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 153946419 341 NVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQ 388
Cdd:cd19723    6 NERERNRVKLVNLGFATLREHVPNGRANKKMSKVETLRSAVEYIRQLQ 53

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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153946419 342 VLERQRRNELKLSFFALRDEIPEVANNEKAAkvvILKKATECIHSMQLDEQRLLS 396
Cdd:cd11450    9 VSERNRRQKLNQRLFALRSVVPNITKMDKAS---IIKDAISYIQELQYQEKKLEA 60

basic helix-loop-helix (bHLH) domain found in factor in the germline alpha (FIGLA) and similar proteins; FIGLA, also termed FIGalpha, or Class C basic helix-loop-helix protein 8 (bHLHc8), or folliculogenesis-specific basic helix-loop-helix protein, or transcription factor FIGa, is a germ-cell-specific bHLH transcription factor expressed abundantly in female and less so in male germ cells. It is essential for primordial follicle formation and expression of many genes required for folliculogenesis, fertilization and early embryonic survival. FIGLA knockout mice cannot form primordial follicles and lose oocytes rapidly after birth, whereas male gonads are unaffected.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153946419 337 RRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQ 388
Cdd:cd11422    1 RRVANARERERVRNLNSGFSKLRRIVPLIPRDRKPSKVDTLKGATEYIRLLQ 52

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        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153946419 334 NDKRRthNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQ 388
Cdd:cd19743    3 AVERR--NERERNRVKLVNLGFAALRQHVPQGGASKKMSKVETLRSAVEYIRALQ 55

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 153946419 336 KRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSM 387
Cdd:cd19711    1 RRLESNERERQRMHKLNNAFQALREVIPHVRAEKKLSKIETLTLAKNYIKSL 52

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').

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946419 335 DKRRTHNVLERQRRNELKLSFFALRDEIpeVANNEKAAKVVILKKATECIHSMQLDEQRL 394
Cdd:cd18921    5 EKRTAHNAIEKRYRSSINDKIIELKDLV--VGTEAKLNKSAVLRKAIDYIRFLQQSNQKL 62

basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and similar proteins; INO2 is a positive regulatory factor required for depression of the co-regulated phospholipid biosynthetic enzymes in Saccharomyces cerevisiae. It is also involved in the expression of ITR1.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153946419 336 KRRTHNVLERQRRNELKLSFFALRDEI--PEVANNEKAAKVVILKKATECIHSMQLDEQRLLSI 397
Cdd:cd11388    3 KKWKHVEAEKKRRNQIKKGFEDLINLInyPRNNNEKRISKSELLNKAVDDIRGLLKANEQLQEE 66