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Conserved domains on  [gi|14602435|ref|NP_116570|]
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carbohydrate-responsive element-binding protein isoform beta [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NES2-NLS_ChREBP cd21771
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
 81-196 2.36e-86

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), and similar proteins; 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), is a large transcription factor that functions at two levels, nuclear localization and DNA binding. It binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. ChREBP contains 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.


:

Pssm-ID: 439287  Cd Length: 116  Bit Score: 269.53  E-value: 2.36e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  81 SIDPTLTRLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVKRRKSPVCGFVTPLQGPEADAHRKP 160
Cdd:cd21771   1 SIDPTLTRLFECMSLAYSGKLVSPKWKNFKGLRLLWRDKIRLNNAIWRAWYIQYVEKRKNPVCGFVTPLEGSEADEHRKP 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 14602435 161 EAVVLEGNYWKRRIEVVMREYHKWRIYYKKRLRKPS 196
Cdd:cd21771  81 EAVVLEGNYWKRRIEVVMKEYHKWRIYYKKRLRKSS 116
bHLH_SF super family cl00081
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 646-702 9.64e-30

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.


The actual alignment was detected with superfamily member cd19689:

Pssm-ID: 469605  Cd Length: 76  Bit Score: 112.37  E-value: 9.64e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14602435 646 KTENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLK-------------------ERAGLQEEAQQLRDEI 702
Cdd:cd19689   1 KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIKiskattlqktaeyisklqqERAQLQEEAQRLRDQI 76
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 306-633 6.70e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   306 SRLPQPPMPSNFPEPPSFSPVVDSLFSSGTLGPEVPPASSAMTHLSGHSRL-----QARNSCPGPLDSSAFLSSdfllPE 380
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLppgpaAARQASPALPAAPAPPAV----PA 2746

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   381 DPKPRLPPPPVPPPLLHYPPPAKVPGLEPCPPPPFPPMAPPTALLQEEPLFSPRFPFPTVPPA---------PGVSPLPA 451
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAavlapaaalPPAASPAG 2826

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   452 PAAFPPTPQSVPSPAPTPFPIELLPLGYSEPAFGPCFSMPRGKPPAPSPRGQKASPPTLAPATASPPTTAGSNNPCLTQ- 530
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPe 2906

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   531 -LLTAAKPEQALEPPLVSSTLLRSPGSPQETVPEFPCTFLPPTPAPTPPRPPPGPATLAPSRPLLVPKAERLSP------ 603
Cdd:PHA03247 2907 rPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPqpapsr 2986

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 14602435   604 --PAPSGSERR-------------LSGDLSSMPGPGTLSVRVSPP 633
Cdd:PHA03247 2987 eaPASSTPPLTghslsrvsswassLALHEETDPPPVSLKQTLWPP 3031
 
Name Accession Description Interval E-value
NES2-NLS_ChREBP cd21771
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
 81-196 2.36e-86

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), and similar proteins; 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), is a large transcription factor that functions at two levels, nuclear localization and DNA binding. It binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. ChREBP contains 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.


Pssm-ID: 439287  Cd Length: 116  Bit Score: 269.53  E-value: 2.36e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  81 SIDPTLTRLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVKRRKSPVCGFVTPLQGPEADAHRKP 160
Cdd:cd21771   1 SIDPTLTRLFECMSLAYSGKLVSPKWKNFKGLRLLWRDKIRLNNAIWRAWYIQYVEKRKNPVCGFVTPLEGSEADEHRKP 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 14602435 161 EAVVLEGNYWKRRIEVVMREYHKWRIYYKKRLRKPS 196
Cdd:cd21771  81 EAVVLEGNYWKRRIEVVMKEYHKWRIYYKKRLRKSS 116
bHLHzip_MLXIPL cd19689
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) ...
 646-702 9.64e-30

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'.


Pssm-ID: 381532  Cd Length: 76  Bit Score: 112.37  E-value: 9.64e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14602435 646 KTENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLK-------------------ERAGLQEEAQQLRDEI 702
Cdd:cd19689   1 KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIKiskattlqktaeyisklqqERAQLQEEAQRLRDQI 76
PHA03247 PHA03247
large tegument protein UL36; Provisional
 306-633 6.70e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   306 SRLPQPPMPSNFPEPPSFSPVVDSLFSSGTLGPEVPPASSAMTHLSGHSRL-----QARNSCPGPLDSSAFLSSdfllPE 380
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLppgpaAARQASPALPAAPAPPAV----PA 2746

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   381 DPKPRLPPPPVPPPLLHYPPPAKVPGLEPCPPPPFPPMAPPTALLQEEPLFSPRFPFPTVPPA---------PGVSPLPA 451
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAavlapaaalPPAASPAG 2826

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   452 PAAFPPTPQSVPSPAPTPFPIELLPLGYSEPAFGPCFSMPRGKPPAPSPRGQKASPPTLAPATASPPTTAGSNNPCLTQ- 530
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPe 2906

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   531 -LLTAAKPEQALEPPLVSSTLLRSPGSPQETVPEFPCTFLPPTPAPTPPRPPPGPATLAPSRPLLVPKAERLSP------ 603
Cdd:PHA03247 2907 rPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPqpapsr 2986

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 14602435   604 --PAPSGSERR-------------LSGDLSSMPGPGTLSVRVSPP 633
Cdd:PHA03247 2987 eaPASSTPPLTghslsrvsswassLALHEETDPPPVSLKQTLWPP 3031
 
Name Accession Description Interval E-value
NES2-NLS_ChREBP cd21771
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
 81-196 2.36e-86

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), and similar proteins; 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), is a large transcription factor that functions at two levels, nuclear localization and DNA binding. It binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. ChREBP contains 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.


Pssm-ID: 439287  Cd Length: 116  Bit Score: 269.53  E-value: 2.36e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  81 SIDPTLTRLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVKRRKSPVCGFVTPLQGPEADAHRKP 160
Cdd:cd21771   1 SIDPTLTRLFECMSLAYSGKLVSPKWKNFKGLRLLWRDKIRLNNAIWRAWYIQYVEKRKNPVCGFVTPLEGSEADEHRKP 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 14602435 161 EAVVLEGNYWKRRIEVVMREYHKWRIYYKKRLRKPS 196
Cdd:cd21771  81 EAVVLEGNYWKRRIEVVMKEYHKWRIYYKKRLRKSS 116
NES2-NLS_MLXIP cd21772
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
 81-194 1.09e-67

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.


Pssm-ID: 439288  Cd Length: 117  Bit Score: 219.93  E-value: 1.09e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  81 SIDPTLTRLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVKRRKSPVCGFVTPLQGP-EADAHRK 159
Cdd:cd21772   1 SIDASLTKLFECMTLAYSGKLVSPKWKNFKGLKLQWRDKIRLNNAIWRAWYMQYLEKRKNPVCHFVTPLDGSvDVDEHRR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 14602435 160 PEAVVLEGNYWKRRIEVVMREYHKWRIYYKKRLRK 194
Cdd:cd21772  81 PEAIATEGKYWKRRIEIVIREYHKWRTYFKKRLQK 115
NES2-NLS_ChREBP-like cd21739
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
 81-196 7.81e-67

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.


Pssm-ID: 439286  Cd Length: 113  Bit Score: 217.52  E-value: 7.81e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  81 SIDPTLTRLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVKRRKSPVCGFVTPLqgpEADAHRKP 160
Cdd:cd21739   1 AIDESLTKLFKCLTLAYSGKLTSPKWKNFKGLKLRWKDKIRLNNAIWREWHMQFVKKKKPPVCQFAVPL---DDDTHKKP 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 14602435 161 EAVVLEGNYWKRRIEVVMREYHKWRIYYKKRLRKPS 196
Cdd:cd21739  78 EAVVLEGKYWKRRLETVVREYKKWRLFYKDKLAGKT 113
bHLHzip_MLXIPL cd19689
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) ...
 646-702 9.64e-30

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'.


Pssm-ID: 381532  Cd Length: 76  Bit Score: 112.37  E-value: 9.64e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14602435 646 KTENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLK-------------------ERAGLQEEAQQLRDEI 702
Cdd:cd19689   1 KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIKiskattlqktaeyisklqqERAQLQEEAQRLRDQI 76
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
 648-702 4.88e-21

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: 87.72  E-value: 4.88e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14602435 648 ENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLK-------------------ERAGLQEEAQQLRDEI 702
Cdd:cd11405   1 EQRRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQNPNQKvskaamlqkaaeyikslkrERQQMQEEAEQLRQEI 74
bHLHzip_MLXIP cd19688
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and ...
 648-702 1.09e-18

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and similar proteins; MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm.


Pssm-ID: 381531  Cd Length: 72  Bit Score: 80.76  E-value: 1.09e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14602435 648 ENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSL-----------------KERAGLQEEAQQLRDEI 702
Cdd:cd19688   1 KNRRMKHISAEQKRRFNIKICFDTLNSLVSTLKNSKPIsnaitlqktveyiaklqQERTQMQEETKRLREEI 72
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 650-705 6.35e-07

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: 47.29  E-value: 6.35e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14602435 650 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSaQPSLKERAGLQEEA---QQLRDEIEEL 705
Cdd:cd11404   2 RRLNHVRSEKKRRELIKKGYDELCALVPGLD-PQKRTKADILQKAAdwiQELKEENEKL 59
bHLHzip_Mlx cd19687
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar ...
 649-702 3.27e-05

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: 42.79  E-value: 3.27e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14602435 649 NRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSL----------------------KERAGLQEEAQQLRDEI 702
Cdd:cd19687   1 RRREAHTQAEQKRRDAIKKGYDDLQDIVPTCQQQDDIgsqklskatilqrsidyiqflhQQKKKQEEELSALRKEV 76
bHLH_scINO4_like cd11403
basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar ...
 650-721 1.32e-04

basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar proteins; INO4 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. INO4 dimerizes with INO2 and binds to an UAS DNA element to control expression of the genes whose expression is inositol-responsive.


Pssm-ID: 381409  Cd Length: 71  Bit Score: 40.91  E-value: 1.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14602435 650 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKERAGLQEEAQQLRDEIEElNAAInlcQQQLPATGV 721
Cdd:cd11403   2 KKENHISSEHKRREAIREGFDRLCAIVPALSSSQSRSEAVVYVKTVEYLKELYER-RAKL---RSQLRSKGV 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
 306-633 6.70e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   306 SRLPQPPMPSNFPEPPSFSPVVDSLFSSGTLGPEVPPASSAMTHLSGHSRL-----QARNSCPGPLDSSAFLSSdfllPE 380
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLppgpaAARQASPALPAAPAPPAV----PA 2746

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   381 DPKPRLPPPPVPPPLLHYPPPAKVPGLEPCPPPPFPPMAPPTALLQEEPLFSPRFPFPTVPPA---------PGVSPLPA 451
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAavlapaaalPPAASPAG 2826

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   452 PAAFPPTPQSVPSPAPTPFPIELLPLGYSEPAFGPCFSMPRGKPPAPSPRGQKASPPTLAPATASPPTTAGSNNPCLTQ- 530
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPe 2906

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435   531 -LLTAAKPEQALEPPLVSSTLLRSPGSPQETVPEFPCTFLPPTPAPTPPRPPPGPATLAPSRPLLVPKAERLSP------ 603
Cdd:PHA03247 2907 rPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPqpapsr 2986

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 14602435   604 --PAPSGSERR-------------LSGDLSSMPGPGTLSVRVSPP 633
Cdd:PHA03247 2987 eaPASSTPPLTghslsrvsswassLALHEETDPPPVSLKQTLWPP 3031
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
441-642 2.84e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  441 PPAPGVSPLPAPAAFPPTPQSVPSPAPTPFPIELLPLGYSEPAFGPCFSMPRGKPPAPSPRGQKASPPTLAPATASPPTT 520
Cdd:PRK12323 373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAP 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  521 AGSNNPCLTQLLTAAKPEQ----ALEPPLVSSTLLRSPGSPQETVP--EFPCTFLPPTPAPTPPRPPPGPATLAPSRPLL 594
Cdd:PRK12323 453 APAAAPAAAARPAAAGPRPvaaaAAAAPARAAPAAAPAPADDDPPPweELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14602435  595 VPKAER----LSPPAPSGSERRLSGDLSSMPGPGTLSVRVSPPQ-----PILSRGRP 642
Cdd:PRK12323 533 DPDDAFetlaPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMfdgdwPALAARLP 589
PHA03378 PHA03378
EBNA-3B; Provisional
 319-635 4.30e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  319 EPPSFSPVVDSLFSSGTLGP-EVPPASSAMTHlsghsrlQARNSCPGPLDSSAFLSSDFLLPEDPKPRLPPPPVPPPLLH 397
Cdd:PHA03378 552 EPASTEPVHDQLLPAPGLGPlQIQPLTSPTTS-------QLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQW 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  398 YPPPAKVPglepcppppfppmaPPTALLQEEPLFSPRFPFPTVPPAPGVSPLPAPAAFPPTPQSVPSPA--PTPFPIELL 475
Cdd:PHA03378 625 PMPLRPIP--------------MRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTgaNTMLPIQWA 690

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  476 PLGYSEPAFGPCFSMPRGKPPAPSPRGQKAS----PPTLAPATASPPTTAGSNNPCLTQLLTAAKPEQALEPPLVSSTll 551
Cdd:PHA03378 691 PGTMQPPPRAPTPMRPPAAPPGRAQRPAAATgrarPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPA-- 768

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602435  552 RSPGSPQETVPefpctflppTPAPTPPRPPPGPATLAPSRPLLVPKAERLSPPAPSGSERRLSGDLSSMPGPGTLSVRVS 631
Cdd:PHA03378 769 AAPGAPTPQPP---------PQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPS 839


                 ....
gi 14602435  632 PPQP 635
Cdd:PHA03378 840 LKKP 843
bHLH_ScINO2_like cd11388
basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and ...
 650-705 5.48e-03

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.


Pssm-ID: 381394  Cd Length: 68  Bit Score: 36.18  E-value: 5.48e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14602435 650 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLK-ERAGLqeeAQQLRDEIEEL 705
Cdd:cd11388   3 KKWKHVEAEKKRRNQIKKGFEDLINLINYPRNNNEKRiSKSEL---LNKAVDDIRGL 56
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
 651-707 6.22e-03

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: 36.10  E-value: 6.22e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14602435 651 RITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKER--AGLQEEAQQLRDEIEELNA 707
Cdd:cd19682   1 RLRHKKRERERRSELRELFDKLKQLLGLDSDEKASKLAvlTEAIEEIQQLKREEDELQK 59
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
 650-716 9.24e-03

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: 35.99  E-value: 9.24e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14602435 650 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPS------LKERA----GLQEEAQQLRDEIEELNAAINLCQQQL 716
Cdd:cd11400   1 KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKaskvviLKKATeyikQLQQEEKKLEKEKDKLKARNEQLRKKL 77
 
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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