nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), MLX-interacting protein (MLXIP), and similar proteins; This family includes two transcription factors: ChREBP and MLXIP. ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), functions at two levels; nuclear localization and DNA binding. ChREBP binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. MLXIP, also called class E basic helix-loop-helix protein 36 (bHLHe36), transcriptional activator MondoA, or MIR, is a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. MLXIP binds DNA by forming a heterodimer with Max-like protein (MLX), and activates transcription. It binds to the canonical E box sequence 5'-CACGTG-3'. MLXIP plays a role in transcriptional activation of glycolytic target genes and is involved in glucose-responsive gene regulation. Members in this family may contain functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569 103 TIDDSFTKLFECMTLAYSGKLCSPKFKNFRGLKLRLKDKLRLNNIIWREWHMQYVKGQFPVVCQFATPVSDDTHIRPEAV 182
Cdd:cd21739    1 AIDESLTKLFKCLTLAYSGKLTSPKWKNFKGLKLRWKDKIRLNNAIWREWHMQFVKKKKPPVCQFAVPLDDDTHKKPEAV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 919103569 183 VLEGKYWKRKLEVVTAEYKKWRVFYKHRLKCRP 215
Cdd:cd21739   81 VLEGKYWKRRLETVVREYKKWRLFYKDKLAGKT 113

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569  577 PTFNRAKPRTIVPAPTvpPAATIAMTTQPSGTSITQQNTFLAQLLTTGDISgtyPGANITMKTetpasCGGKMFTPIRPA 656
Cdd:pfam05109 551 PTPNATSPTPAVTTPT--PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS---PQANTTNHT-----LGGTSSTPVVTS 620

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 919103569  657 PPV-STTAVTT---NSMSMIAAVASLENSSMSSPLS 688
Cdd:pfam05109 621 PPKnATSAVTTgqhNITSSSTSSMSLRPSSISETLS 656

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), MLX-interacting protein (MLXIP), and similar proteins; This family includes two transcription factors: ChREBP and MLXIP. ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), functions at two levels; nuclear localization and DNA binding. ChREBP binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. MLXIP, also called class E basic helix-loop-helix protein 36 (bHLHe36), transcriptional activator MondoA, or MIR, is a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. MLXIP binds DNA by forming a heterodimer with Max-like protein (MLX), and activates transcription. It binds to the canonical E box sequence 5'-CACGTG-3'. MLXIP plays a role in transcriptional activation of glycolytic target genes and is involved in glucose-responsive gene regulation. Members in this family may contain functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569 103 TIDDSFTKLFECMTLAYSGKLCSPKFKNFRGLKLRLKDKLRLNNIIWREWHMQYVKGQFPVVCQFATPVSDDTHIRPEAV 182
Cdd:cd21739    1 AIDESLTKLFKCLTLAYSGKLTSPKWKNFKGLKLRWKDKIRLNNAIWREWHMQFVKKKKPPVCQFAVPLDDDTHKKPEAV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 919103569 183 VLEGKYWKRKLEVVTAEYKKWRVFYKHRLKCRP 215
Cdd:cd21739   81 VLEGKYWKRRLETVVREYKKWRLFYKDKLAGKT 113

Helix-loop-helix DNA-binding domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 919103569  763 RRVSHISAEQKRRGNIKGGFDVLHTLIPALiqNPNAKISKAQMLQKTAEYCKKLK 817
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTL--PPDKKLSKAEILRLAIEYIKHLQ 53

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569  577 PTFNRAKPRTIVPAPTvpPAATIAMTTQPSGTSITQQNTFLAQLLTTGDISgtyPGANITMKTetpasCGGKMFTPIRPA 656
Cdd:pfam05109 551 PTPNATSPTPAVTTPT--PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS---PQANTTNHT-----LGGTSSTPVVTS 620

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 919103569  657 PPV-STTAVTT---NSMSMIAAVASLENSSMSSPLS 688
Cdd:pfam05109 621 PPKnATSAVTTgqhNITSSSTSSMSLRPSSISETLS 656

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), MLX-interacting protein (MLXIP), and similar proteins; This family includes two transcription factors: ChREBP and MLXIP. ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), functions at two levels; nuclear localization and DNA binding. ChREBP binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. MLXIP, also called class E basic helix-loop-helix protein 36 (bHLHe36), transcriptional activator MondoA, or MIR, is a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. MLXIP binds DNA by forming a heterodimer with Max-like protein (MLX), and activates transcription. It binds to the canonical E box sequence 5'-CACGTG-3'. MLXIP plays a role in transcriptional activation of glycolytic target genes and is involved in glucose-responsive gene regulation. Members in this family may contain functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569 103 TIDDSFTKLFECMTLAYSGKLCSPKFKNFRGLKLRLKDKLRLNNIIWREWHMQYVKGQFPVVCQFATPVSDDTHIRPEAV 182
Cdd:cd21739    1 AIDESLTKLFKCLTLAYSGKLTSPKWKNFKGLKLRWKDKIRLNNAIWREWHMQFVKKKKPPVCQFAVPLDDDTHKKPEAV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 919103569 183 VLEGKYWKRKLEVVTAEYKKWRVFYKHRLKCRP 215
Cdd:cd21739   81 VLEGKYWKRRLETVVREYKKWRLFYKDKLAGKT 113

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in MLX-interacting protein (MLXIP), and similar proteins; MLXIP, also called class E basic helix-loop-helix protein 36 (bHLHe36), transcriptional activator MondoA, or MIR, is a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. It binds DNA by forming a heterodimer with Max-like protein (MLX) and activates transcription. It binds to the canonical E box sequence 5'-CACGTG-3'. MLXIP plays a role in transcriptional activation of glycolytic target genes and is involved in glucose-responsive gene regulation. MLXIP may contain functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569 103 TIDDSFTKLFECMTLAYSGKLCSPKFKNFRGLKLRLKDKLRLNNIIWREWHMQYVKGQFPVVCQFATP----VSDDTHIR 178
Cdd:cd21772    1 SIDASLTKLFECMTLAYSGKLVSPKWKNFKGLKLQWRDKIRLNNAIWRAWYMQYLEKRKNPVCHFVTPldgsVDVDEHRR 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 919103569 179 PEAVVLEGKYWKRKLEVVTAEYKKWRVFYKHRLK 212
Cdd:cd21772   81 PEAIATEGKYWKRRIEIVIREYHKWRTYFKKRLQ 114

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) and similar proteins; 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 919103569 761 EHRRVSHISAEQKRRGNIKGGFDVLHTLIPALIQNPNAKISKAQMLQKTAEYCKKLKSDRKQMQDEAEILRQEI 834
Cdd:cd19689    3 ETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIKISKATTLQKTAEYISKLQQERAQLQEEAQRLRDQI 76

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 919103569 762 HRRVSHISAEQKRRGNIKGGFDVLHTLIPALIQNPNA---KISKAQMLQKTAEYCKKLKSDRKQMQDEAEILRQEI 834
Cdd:cd19687    1 RRREAHTQAEQKRRDAIKKGYDDLQDIVPTCQQQDDIgsqKLSKATILQRSIDYIQFLHQQKKKQEEELSALRKEV 76

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 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPALIQNpnaKISKAQMLQKTAEYCKKLKsdrkqmqDEAEILRQEIESLNSAI 841
Cdd:cd11404    2 RRLNHVRSEKKRRELIKKGYDELCALVPGLDPQ---KRTKADILQKAADWIQELK-------EENEKLEEQLDELKEAA 70

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 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPALIQNPNAKISKAQMLQKTAEYCKKLKSDRKQMQDEAE 828
Cdd:cd11388    3 KKWKHVEAEKKRRNQIKKGFEDLINLINYPRNNNEKRISKSELLNKAVDDIRGLLKANEQLQEEIN 68

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPALIQNPNA-------------KISKAQMLQKTAEYCKKLKSDRKQMQDEAEI 829
Cdd:cd11395    3 KRLPHNAIEKRYRSNLNTKIERLRDAIPSLRSPEGKsddgglgglapttKLSKATILTKAIEYIRHLEQENERLEEENEE 82

                 ....*
gi 919103569 830 LRQEI 834
Cdd:cd11395   83 LRQQV 87

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 919103569 757 QQYKEHRRVSHISAEQKRRGNIKGGFDVLHTLIPaliqNPNAKISKAQMLQKTAEYCKKLKSDRKQMQDEA---EILRQE 833
Cdd:cd11398    1 EEWHRQRRDNHKEVERRRRENINEGINELAALVP----GNAREKNKGAILARAVEYIQELQETEAKNIEKWtleKLLTDQ 76

                 ....*....
gi 919103569 834 IESLNSAIN 842
Cdd:cd11398   77 AIAELAALN 85

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPALiqnPNAKISKAQMLQKTAEYCKKL-KSDRKQMQDEAEILRQ 832
Cdd:cd11406    1 KRAHHNALERKRRDHIKDSFHSLRDSVPSL---QGEKASRAQILKKATEYIQYMrRKNHTHQQDIDDLKRQ 68

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription factors and similar proteins; bHLH proteins are the second largest class of plant transcription factors that regulate transcription of genes that are involve in many essential physiological and developmental process. bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. The Arabidopsis bHLH proteins that have been characterized so far have roles in regulation of fruit dehiscence, cell development (carpel, anther and epidermal), phytochrome signaling, flavonoid biosynthesis, hormone signaling and stress responses.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919103569 767 HISAEQKRRGNIKGGFDVLHTLIPaliqnPNAKISKAQMLQKTAEYCKKLKSDRKQMQ 824
Cdd:cd11393    1 HSIAERKRREKINERIRALRSLVP-----NGGKTDKASILDEAIEYIKFLQEQVKVLS 53

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPALIQNPNAkiSKAQMLQKTAEYCKKLKSDRKQMQDEAEILRQEIESL 837
Cdd:cd11456    5 RRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKA--AKVVILKKATEYVHSLQAEEQKLLLEKEKLQARQQQL 77

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BES1-interacting Myc-like proteins (BIMs) and similar proteins; The family includes Arabidopsis thaliana BIM1 and its homologs (BIM2 and BIM3), which are bHLH transcription factors that interact with BES1 to regulate transcription of Brassinosteroid (BR)-induced gene. BR regulates many growth and developmental processes such as cell elongation, vascular development, senescence stress responses, and photomorphogenesis. BIM1 heterodimerize with BES1 and bind to E-box sequences present in many BR-induced promoters to regulated BR-induced genes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPaliqNPNAKISKAQMLQKTAEYCKKLKSDRKQMQDEAEILRQE 833
Cdd:cd11453    3 PRSKHSATEQRRRSKINERLQALRDLIP----HSDQKRDKASFLLEVIEYIQALQEKVAKLEEQVQGWGGE 69

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919103569 764 RVSHISAEQKRRGNIKGGFDVLHTLIPAliqNPNAKISKAQMLQKTAEYCKKLKSDRKQMQDEAEILR 831
Cdd:cd19682    1 RLRHKKRERERRSELRELFDKLKQLLGL---DSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARLT 65

basic helix-loop-helix (bHLH) domain found in achaete-scute complex-like (ASCL) family; The achaete-scute complex-like (ASCL, also known as achaete-scute complex homolog or ASH) family of bHLH transcription factors, ASCL1-5, have been implicated in cell fate specification and differentiation. They are critical for proper development of the nervous system. The deregulation of ASCL plays a key role in psychiatric and neurological disorders. 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. 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. ASCL-3, also termed Class A basic helix-loop-helix protein 42 (bHLHa42), or bHLH transcriptional regulator Sgn-1, or achaete-scute homolog 3 (ASH-3), is a bHLH transcription factor specifically localized in the duct cells of the salivary glands. It may act as transcriptional repressor that inhibits myogenesis. The family also includes Drosophila melanogaster achaete-scute complex (AS-C) proteins, which consists of 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919103569 755 ERQQYKEHRRVSHISaeqkrrgnikGGFDVLHTLIPALiqNPNAKISKAQMLQKTAEYCKKLK 817
Cdd:cd11418    3 ARRNERERRRVQAVN----------DAFDRLRQHVPYL--KRRKKLSKVKTLRRAIEYIRHLQ 53

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 2 (USF2) and similar proteins; USF2, also termed Class B basic helix-loop-helix protein 12 (bHLHb12), or major late transcription factor 2, or FOS-interacting protein (FIP), or upstream transcription factor 2, is a bHLHzip transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919103569 756 RQQYKEHRRVSHISAEQKRRGNIKGGFDVLHTLIPAL-IQNPNAKISKAQMLQKTAEYCKKLKSDRKQMQD---EAEILR 831
Cdd:cd18923    1 RTPRDERRRAQHNEVERRRRDKINNWIVQLSKIIPDCnTDNSKTGASKGGILSKACDYIRELRQTNQRMQEtykEAERLQ 80

basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster enhancer of split mbeta protein (ESMB) and similar proteins; ESMB, also termed E(spl)mbeta, or HLH-mbeta, or split locus enhancer protein mA, is a bHLH-O transcriptional repressor of genes that require a bHLH protein for their transcription. It is involved in the neural-epidermal lineage decision during early neurogenesis. The family also includes Enhancer of split m7 protein (also known as E(spl)m7), which acts as a transcriptional repressor that participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919103569 760 KEHRRVSHISAEQKRRGNIKGGFDVLHTLI-PALIQ--NPNAKISKAQMLQKTAEYCKKLKSDRK 821
Cdd:cd19741    5 YQYRKVTKPLLERKRRARINKCLDELKDLMvEALATeaENVSKLEKADILELTVRHLKKLRRQKS 69

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar proteins; NAI1, also termed AtbHLH20, or EN 27, is a bHLH transcription activator that regulates the expression of at least NAI2, PYK10 and PBP1. It is required for and mediates the formation of endoplasmic reticulum bodies (ER bodies). It plays a role in the symbiotic interactions with the endophytes of the Sebacinaceae fungus family, such as Piriformospora indica and Sebacina.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919103569 767 HISAEQKRRGNIKGGFDVLHTLIPALiqnpnAKISKAQMLQKTAEYCKKLKSDRKQMQDEAEILRQEIESL 837
Cdd:cd11452    6 HILAERKRREKLSQRFIALSALVPGL-----KKMDKASVLGDAIKHIKQLQERVKELEEEKKEKRLMSVVI 71

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 919103569 763 RRVSHISAEQKRRGNIKGGFDVLHTLIPAL------------------IQNPNAKISKAQMLQKTAEYCKKLKSDRKQMQ 824
Cdd:cd11399    3 KKTAHNMIEKRYRSNINDRIAELRDSVPALreayksargededeedlgGLTPATKLNKATILSKATEYIRHLEKKNKRLS 82

                         90
                 ....*....|...
gi 919103569 825 DEAEILRQEIESL 837
Cdd:cd11399   83 RENASLRERLAAH 95