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Conserved domains on  [gi|115313792|gb|AAI24205|]
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V-myc myelocytomatosis viral oncogene homolog 1, lung carcinoma derived (avian) b [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Myc_N super family cl03082
Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper ...
18-273 8.69e-63

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


The actual alignment was detected with superfamily member pfam01056:

Pssm-ID: 460045  Cd Length: 339  Bit Score: 205.02  E-value: 8.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792   18 EYDQYQHYFYDDhnlDEDFF----KSTAPSEDIWKKFELVPTPPMSPVR--ILEGSGPSPGDRLEWVSQFLGQDD-EQEG 90
Cdd:pfam01056  14 DYDSLQPCFYPE---EEDFYfsglQPPAPSEDIWKKFELLPTPPLSPSRrsSLSSPFPSTADQLEMVTELLGADLvNQSF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792   91 LCKLNAEETLenLSSIIIQDCMWSSFSASQQLEKVVSERL-SCSAQSKLSGKAQCVPADVPA------------------ 151
Cdd:pfam01056  91 ICDPDEDDSF--LKSIIIQDCMWSGFSAAAKLEKVVSEKLaSGQAARKEGAATLAAGAASSAgrahsgsagggrsssgyl 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792  152 --LNSLATDCVDPAAVLTFPLSSSCKKQV-----------------------SSGSESRTDSS----------------- 189
Cdd:pfam01056 169 qdLSHSASECVDPSVVFPFPLNKREKAPVppapspalaldppatpprssgssSSSGDSKGLSSsgedtlsdsddeeeeee 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792  190 -DDEEIDVVTVEHKQNKSRlvnaRKPVTITVRA-----DPHDP-CMKRFHISIHqqQHNYAArsPDSYPEEEPPRKKIRQ 262
Cdd:pfam01056 249 eEEEEIDVVTVEKRQPSSK----RKEVSTLTTAlghsrPQHSPlVLKRCHVIIH--QHNYAA--PPSTRSEDPPQKRLKL 320
                         330
                  ....*....|....*....
gi 115313792  263 E--------IVQPRLASTP 273
Cdd:pfam01056 321 EssgrvlkqISNNRKCSSP 339
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
316-404 7.65e-39

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


:

Pssm-ID: 381463 [Multi-domain]  Cd Length: 89  Bit Score: 134.54  E-value: 7.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 316 DCEDTDKRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLL 395
Cdd:cd11457    1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLL 80

                 ....*....
gi 115313792 396 RRLAELKRA 404
Cdd:cd11457   81 RRIAQLKGR 89
 
Name Accession Description Interval E-value
Myc_N pfam01056
Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper ...
18-273 8.69e-63

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


Pssm-ID: 460045  Cd Length: 339  Bit Score: 205.02  E-value: 8.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792   18 EYDQYQHYFYDDhnlDEDFF----KSTAPSEDIWKKFELVPTPPMSPVR--ILEGSGPSPGDRLEWVSQFLGQDD-EQEG 90
Cdd:pfam01056  14 DYDSLQPCFYPE---EEDFYfsglQPPAPSEDIWKKFELLPTPPLSPSRrsSLSSPFPSTADQLEMVTELLGADLvNQSF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792   91 LCKLNAEETLenLSSIIIQDCMWSSFSASQQLEKVVSERL-SCSAQSKLSGKAQCVPADVPA------------------ 151
Cdd:pfam01056  91 ICDPDEDDSF--LKSIIIQDCMWSGFSAAAKLEKVVSEKLaSGQAARKEGAATLAAGAASSAgrahsgsagggrsssgyl 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792  152 --LNSLATDCVDPAAVLTFPLSSSCKKQV-----------------------SSGSESRTDSS----------------- 189
Cdd:pfam01056 169 qdLSHSASECVDPSVVFPFPLNKREKAPVppapspalaldppatpprssgssSSSGDSKGLSSsgedtlsdsddeeeeee 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792  190 -DDEEIDVVTVEHKQNKSRlvnaRKPVTITVRA-----DPHDP-CMKRFHISIHqqQHNYAArsPDSYPEEEPPRKKIRQ 262
Cdd:pfam01056 249 eEEEEIDVVTVEKRQPSSK----RKEVSTLTTAlghsrPQHSPlVLKRCHVIIH--QHNYAA--PPSTRSEDPPQKRLKL 320
                         330
                  ....*....|....*....
gi 115313792  263 E--------IVQPRLASTP 273
Cdd:pfam01056 321 EssgrvlkqISNNRKCSSP 339
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
316-404 7.65e-39

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


Pssm-ID: 381463 [Multi-domain]  Cd Length: 89  Bit Score: 134.54  E-value: 7.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 316 DCEDTDKRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLL 395
Cdd:cd11457    1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLL 80

                 ....*....
gi 115313792 396 RRLAELKRA 404
Cdd:cd11457   81 RRIAQLKGR 89
HLH pfam00010
Helix-loop-helix DNA-binding domain;
322-374 3.18e-13

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 63.63  E-value: 3.18e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115313792  322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLH 374
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
327-373 9.44e-12

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 59.54  E-value: 9.44e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 115313792   327 NFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTL 373
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSL 47
 
Name Accession Description Interval E-value
Myc_N pfam01056
Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper ...
18-273 8.69e-63

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


Pssm-ID: 460045  Cd Length: 339  Bit Score: 205.02  E-value: 8.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792   18 EYDQYQHYFYDDhnlDEDFF----KSTAPSEDIWKKFELVPTPPMSPVR--ILEGSGPSPGDRLEWVSQFLGQDD-EQEG 90
Cdd:pfam01056  14 DYDSLQPCFYPE---EEDFYfsglQPPAPSEDIWKKFELLPTPPLSPSRrsSLSSPFPSTADQLEMVTELLGADLvNQSF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792   91 LCKLNAEETLenLSSIIIQDCMWSSFSASQQLEKVVSERL-SCSAQSKLSGKAQCVPADVPA------------------ 151
Cdd:pfam01056  91 ICDPDEDDSF--LKSIIIQDCMWSGFSAAAKLEKVVSEKLaSGQAARKEGAATLAAGAASSAgrahsgsagggrsssgyl 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792  152 --LNSLATDCVDPAAVLTFPLSSSCKKQV-----------------------SSGSESRTDSS----------------- 189
Cdd:pfam01056 169 qdLSHSASECVDPSVVFPFPLNKREKAPVppapspalaldppatpprssgssSSSGDSKGLSSsgedtlsdsddeeeeee 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792  190 -DDEEIDVVTVEHKQNKSRlvnaRKPVTITVRA-----DPHDP-CMKRFHISIHqqQHNYAArsPDSYPEEEPPRKKIRQ 262
Cdd:pfam01056 249 eEEEEIDVVTVEKRQPSSK----RKEVSTLTTAlghsrPQHSPlVLKRCHVIIH--QHNYAA--PPSTRSEDPPQKRLKL 320
                         330
                  ....*....|....*....
gi 115313792  263 E--------IVQPRLASTP 273
Cdd:pfam01056 321 EssgrvlkqISNNRKCSSP 339
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
316-404 7.65e-39

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


Pssm-ID: 381463 [Multi-domain]  Cd Length: 89  Bit Score: 134.54  E-value: 7.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 316 DCEDTDKRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLL 395
Cdd:cd11457    1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLL 80

                 ....*....
gi 115313792 396 RRLAELKRA 404
Cdd:cd11457   81 RRIAQLKGR 89
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
322-379 4.97e-23

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: 91.84  E-value: 4.97e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 115313792 322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQ 379
Cdd:cd11400    1 KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKK 58
bHLHzip_N-Myc_like cd11456
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins; N-Myc, ...
318-402 3.13e-19

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


Pssm-ID: 381462 [Multi-domain]  Cd Length: 87  Bit Score: 81.87  E-value: 3.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 318 EDTDKRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLLRR 397
Cdd:cd11456    1 EDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEQKLLLEKEKLQARQQQLLKK 80

                 ....*
gi 115313792 398 LAELK 402
Cdd:cd11456   81 IEQAR 85
bHLHzip_c-Myc cd11458
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, ...
318-401 1.56e-17

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, also termed Myc proto-oncogene protein, or Class E basic helix-loop-helix protein 39 (bHLHe39), or transcription factor p64, a bHLHZip proto-oncogene protein that functions as a transcription factor, which binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. It activates the transcription of growth-related genes.


Pssm-ID: 381464 [Multi-domain]  Cd Length: 84  Bit Score: 76.84  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 318 EDTDKRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLLRR 397
Cdd:cd11458    1 EENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQLRRRREQLKHR 80

                 ....
gi 115313792 398 LAEL 401
Cdd:cd11458   81 LEQL 84
HLH pfam00010
Helix-loop-helix DNA-binding domain;
322-374 3.18e-13

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 63.63  E-value: 3.18e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115313792  322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLH 374
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
327-373 9.44e-12

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 59.54  E-value: 9.44e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 115313792   327 NFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTL 373
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSL 47
bHLHzip_Max cd11406
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, ...
322-383 1.52e-09

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, also termed Class D basic helix-loop-helix protein 4 (bHLHd4), or Myc-associated factor X, is a bHLHZip transcription regulator that forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a transcriptional repressor. Max homodimer bind DNA but is transcriptionally inactive. Targeted deletion of max results in early embryonic lethality in mice.


Pssm-ID: 381412  Cd Length: 69  Bit Score: 53.89  E-value: 1.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115313792 322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLvDCPKTPKVVILTKATEYLRTLhvsdRQKAQE 383
Cdd:cd11406    1 KRAHHNALERKRRDHIKDSFHSLRDSVPSL-QGEKASRAQILKKATEYIQYM----RRKNHT 57
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
330-374 1.09e-08

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 50.60  E-value: 1.09e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 115313792 330 ERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLH 374
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQ 45
bHLHzip_scHMS1_like cd11399
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae transcription ...
320-383 1.20e-07

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


Pssm-ID: 381405 [Multi-domain]  Cd Length: 96  Bit Score: 49.39  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 320 TDKRKTHNFLERKRRNDLRSRFLALRDEIP--------------------GLVDCPKTPKVVILTKATEYLRTLHVSDRQ 379
Cdd:cd11399    1 PSKKTAHNMIEKRYRSNINDRIAELRDSVPalreayksargededeedlgGLTPATKLNKATILSKATEYIRHLEKKNKR 80

                 ....
gi 115313792 380 KAQE 383
Cdd:cd11399   81 LSRE 84
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
322-383 3.71e-07

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: 47.27  E-value: 3.71e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115313792 322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCP--KTPKVVILTKATEYLRTLHvSDRQKAQE 383
Cdd:cd11405    3 RRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQNPnqKVSKAAMLQKAAEYIKSLK-RERQQMQE 65
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
323-373 1.29e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family; The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381525 [Multi-domain]  Cd Length: 65  Bit Score: 45.34  E-value: 1.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPGLVDcPKTPKVVILTKATEYLRTL 373
Cdd:cd19682    1 RLRHKKRERERRSELRELFDKLKQLLGLDSD-EKASKLAVLTEAIEEIQQL 50
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
322-382 1.37e-06

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: 45.37  E-value: 1.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115313792 322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLvDCPKTPKVVILTKATEYLRTLH-VSDRQKAQ 382
Cdd:cd11404    2 RRLNHVRSEKKRRELIKKGYDELCALVPGL-DPQKRTKADILQKAADWIQELKeENEKLEEQ 62
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
323-404 1.97e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar proteins; Mnt, also termed Class D basic helix-loop-helix protein 3 (bHLHd3), or Myc antagonist MNT, or protein ROX, is a bHLHZip transcriptional repressor that binds DNA as a heterodimer with MAX. It binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'. Mnt has an important role as an antagonist and regulator of Myc activities and it is a potential tumor suppressor. Mnt is ubiquitously expressed. Mnt-deficient mice shown to exhibit early postnatal lethality.


Pssm-ID: 381408 [Multi-domain]  Cd Length: 77  Bit Score: 45.39  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPGLvDCPKTPKVVILTKATEYLRTLHVSDRQKAQEkkqlkskqqqlLRRLAELK 402
Cdd:cd11402    3 REVHNKLEKNRRAHLKECFETLKRQIPNL-DDKKTSNLNILRSALRYIQILKRKEKEYEHE-----------MERLAREK 70

                 ..
gi 115313792 403 RA 404
Cdd:cd11402   71 IA 72
bHLH_AtPIF_like cd11445
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting ...
326-373 9.88e-06

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting factors (PIFs) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as PIFs, ALC, PIL1, SPATULA, and UNE10. PIFs (PIF1, PIF3, PIF4, PIF5, PIF6 and PIF7) have been shown to control light-regulated gene expression. They directly bind to the photoactivated phytochromes and are degraded in response to light signals. ALC, also termed AtbHLH73, or protein ALCATRAZ, or EN 98, is required for the dehiscence of fruit, especially for the separation of the valve cells from the replum. It promotes the differentiation of a strip of labile non-lignified cells sandwiched between layers of lignified cells. PIL1, also termed AtbHLH124, or protein phytochrome interacting factor 3-like 1, or EN 110, is involved in responses to transient and long-term shade. It is required for the light-mediated inhibition of hypocotyl elongation and necessary for rapid light-induced expression of the photomorphogenesis- and circadian-related gene APRR9. PIL1 seems to play a role in multiple PHYB responses, such as flowering transition and petiole elongation. SPATULA, also termed AtbHLH24, or EN 99, plays a role in floral organogenesis. It promotes the growth of carpel margins and of pollen tract tissues derived from them. UNE10, also termed AtbHLH16, or protein UNFERTILIZED EMBRYO SAC 10, or EN 99, is required during the fertilization of ovules by pollen.


Pssm-ID: 381451  Cd Length: 64  Bit Score: 42.74  E-value: 9.88e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 115313792 326 HNFLERKRRNDLRSRFLALRDEIPglvDCPKTPKVVILTKATEYLRTL 373
Cdd:cd11445    6 HNLSERRRRDRINEKMKALQELIP---NCNKTDKASMLDEAIEYLKSL 50
bHLHzip_MXI1 cd18930
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and ...
323-401 4.80e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and similar proteins; MXI1, also termed Max interactor 1, or Class C basic helix-loop-helix protein 11 (bHLHc11), is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX. It plays an important role in the regulation of cell proliferation.


Pssm-ID: 381500 [Multi-domain]  Cd Length: 80  Bit Score: 41.52  E-value: 4.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLLRRLAEL 401
Cdd:cd18930    2 RSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRFLKRRLEQL 80
bHLH_AtbHLH_like cd11393
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription ...
326-374 5.37e-05

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.


Pssm-ID: 381399 [Multi-domain]  Cd Length: 53  Bit Score: 40.63  E-value: 5.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 115313792 326 HNFLERKRRNDLRSRFLALRDEIPGlvdCPKTPKVVILTKATEYLRTLH 374
Cdd:cd11393    1 HSIAERKRREKINERIRALRSLVPN---GGKTDKASILDEAIEYIKFLQ 46
bHLHzip_SREBP_like cd11395
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
322-383 8.22e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family and similar proteins; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box. The family also includes Saccharomyces cerevisiae transcription factor HMS1 (also termed high-copy MEP suppressor protein 1) and serine-rich protein TYE7. HMS1 is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation. TYE7, also termed basic-helix-loop-helix protein SGC1, is a putative bHLHzip transcription activator required for Ty1-mediated glycolytic gene expression. TYE7 N-terminal is extremely rich in serine residues. It binds DNA on E-box motifs, 5'-CANNTG-3'. TYE7 is not essential for growth.


Pssm-ID: 381401 [Multi-domain]  Cd Length: 87  Bit Score: 41.16  E-value: 8.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115313792 322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTP---------------KVVILTKATEYLRTLHVSDRQKAQE 383
Cdd:cd11395    3 KRLPHNAIEKRYRSNLNTKIERLRDAIPSLRSPEGKSddgglgglapttklsKATILTKAIEYIRHLEQENERLEEE 79
bHLHzip_SREBP1 cd18921
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
321-383 8.59e-05

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


Pssm-ID: 381491  Cd Length: 75  Bit Score: 40.65  E-value: 8.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115313792 321 DKRKTHNFLERKRRNDLRSRFLALRDEIPGLVdcPKTPKVVILTKATEYLRTLHVSDRQKAQE 383
Cdd:cd18921    5 EKRTAHNAIEKRYRSSINDKIIELKDLVVGTE--AKLNKSAVLRKAIDYIRFLQQSNQKLKQE 65
bHLHzip_SREBP2 cd18922
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
321-383 1.81e-04

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


Pssm-ID: 381492 [Multi-domain]  Cd Length: 77  Bit Score: 39.94  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115313792 321 DKRKTHNFLERKRRNDLRSRFLALRDEIPGlvDCPKTPKVVILTKATEYLRTLHVSDRQKAQE 383
Cdd:cd18922    5 ERRTTHNIIEKRYRSSINDKIIELKDLVMG--TDAKMHKSGVLRKAIDYIKYLQQVNHKLRQE 65
bHLH_AtTT8_like cd11451
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 ...
326-373 3.03e-04

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 (TT8) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as TT8, EGL1, and GL3. TT8, also termed AtbHLH42, or EN 32, is involved in the control of flavonoid pigmentation and plays a key role in regulating leucoanthocyanidin reductase (BANYULS) and dihydroflavonol-4-reductase (DFR). EGL1, also termed AtbHLH2, or EN 30, or AtMYC146, or protein enhancer of GLABRA 3, is involved in epidermal cell fate specification and regulates negatively stomata formation but promotes trichome formation. GL3, also termed AtbHLH1, or AtMYC6, or protein shapeshifter, or EN 31, is involved in epidermal cell fate specification. It regulates negatively stomata formation, but, in association with TTG1 and MYB0/GL1, promotes trichome formation, branching and endoreplication.


Pssm-ID: 381457  Cd Length: 75  Bit Score: 38.94  E-value: 3.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 115313792 326 HNFLERKRRNDLRSRFLALRDEIPGLVdcpKTPKVVILTKATEYLRTL 373
Cdd:cd11451    6 HAMAERRRREKLNERFITLRSMVPFVT---KMDKVSILGDAIEYLKQL 50
bHLHzip_SREBP cd11394
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
320-383 3.11e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box.


Pssm-ID: 381400 [Multi-domain]  Cd Length: 73  Bit Score: 38.79  E-value: 3.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115313792 320 TDKRKTHNFLERKRRNDLRSRFLALRDEIPGlvDCPKTPKVVILTKATEYLRTLHVSDRQKAQE 383
Cdd:cd11394    4 VEKRSAHNAIEKRYRSSINDRIIELKDLVVG--PDAKMNKSAVLRKAIDYIRYLQKVNQKLKQE 65
bHLH_AtNAI1_like cd11452
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar ...
324-373 4.31e-04

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.


Pssm-ID: 381458 [Multi-domain]  Cd Length: 75  Bit Score: 38.60  E-value: 4.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 115313792 324 KTHNFLERKRRNDLRSRFLALRDEIPGLvdcPKTPKVVILTKATEYLRTL 373
Cdd:cd11452    4 QDHILAERKRREKLSQRFIALSALVPGL---KKMDKASVLGDAIKHIKQL 50
bHLHzip_spESC1_like cd19690
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) ...
323-383 1.19e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins; spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381533  Cd Length: 65  Bit Score: 37.05  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPgLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQE 383
Cdd:cd19690    1 RVSHKLAERKRRKEMKELFEDLRDALP-QERGTKASKWEILTKAISYIQQLKRHIRELRSE 60
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
323-398 1.49e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad family (Mad1, Mxi, Mad3, and Mad4) bear the bHLHzip domain (also known as basic-helix-loop-helix-leucine-zipper or bHLH-LZ domain), which mediates heterodimerization to Max and the sequence-specific DNA binding ability to E-box DNA. Mad family proteins can repress transcription at the E-box through their interaction with co-repressors. Mad family proteins antagonize Myc function in transactivation and transformation and they are growth/tumor suppressors. The developmental phenotypes of the individual Mad family member knockout mice are relatively mild- all these mice have been shown to be viable and normal.


Pssm-ID: 381407 [Multi-domain]  Cd Length: 76  Bit Score: 37.19  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHVSDRQKAQEKKQLKSKQQQLLRRL 398
Cdd:cd11401    1 RSTHNELEKNRRAHLRLCLERLKELVPLGPDATRHTTLSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQRELKRRL 76
bHLH_TS cd11390
tissue specific basic helix-loop-helix (bHLH-TS) domain family; Tissue specific bHLH domain ...
323-373 3.17e-03

tissue specific basic helix-loop-helix (bHLH-TS) domain family; Tissue specific bHLH domain family includes transcription regulators whose expression are restricted to certain tissues. They are involved in cell-fate determination and process in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis and include proteins from myogenic regulatory factor (MRF) family, twist-related protein (TWIST) family, scleraxis-like family, heart- and neural crest derivatives-expressed protein (HAND) family, helix-loop-helix protein (HEN) family, musculin-like family, germline alpha (FIGLA) family, T-cell acute lymphocytic leukemia protein/ lymphoblastic leukemia-derived sequence (TAL/LYL) family, ovary, uterus and testis protein (OUT) family, mesoderm posterior protein (Mesp) family, muscle, intestine and stomach expression 1 (MIST-1) family, protein atonal homologs (ATOH) family, neurogenin (NGN) family, neurogenic differentiation factor (NeuroD) family, achaete-scute complex-like (ASCL) family, Fer3-like protein (FERD3L)-like family, and Oligodendrocyte lineage genes (OLIG) family of transcription factors.


Pssm-ID: 381396 [Multi-domain]  Cd Length: 55  Bit Score: 35.63  E-value: 3.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTL 373
Cdd:cd11390    1 RNAANARERRRMHDLNDAFEALRKVLPTVPPDKKLSKIETLRLAINYIAAL 51
bHLH_TS_ASCL cd11418
basic helix-loop-helix (bHLH) domain found in achaete-scute complex-like (ASCL) family; The ...
330-373 5.24e-03

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.


Pssm-ID: 381424 [Multi-domain]  Cd Length: 56  Bit Score: 34.89  E-value: 5.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 115313792 330 ERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTL 373
Cdd:cd11418    9 ERRRVQAVNDAFDRLRQHVPYLKRRKKLSKVKTLRRAIEYIRHL 52
bHLH_TS_FIGLA cd11422
basic helix-loop-helix (bHLH) domain found in factor in the germline alpha (FIGLA) and similar ...
323-375 5.61e-03

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.


Pssm-ID: 381428  Cd Length: 56  Bit Score: 35.02  E-value: 5.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKTPKVVILTKATEYLRTLHV 375
Cdd:cd11422    1 RRVANARERERVRNLNSGFSKLRRIVPLIPRDRKPSKVDTLKGATEYIRLLQR 53
bHLHzip_USF2 cd18923
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 2 (USF2) ...
319-383 6.39e-03

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.


Pssm-ID: 381493  Cd Length: 80  Bit Score: 35.45  E-value: 6.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115313792 319 DTDKRKTHNFLERKRRNDLRSRFLALRDEIPGL-VDCPKT--PKVVILTKATEYLRTLHVSDrQKAQE 383
Cdd:cd18923    5 DERRRAQHNEVERRRRDKINNWIVQLSKIIPDCnTDNSKTgaSKGGILSKACDYIRELRQTN-QRMQE 71
bHLH_ScINO2_like cd11388
basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and ...
322-383 7.04e-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: 35.02  E-value: 7.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115313792 322 KRKTHNFLERKRRNDLRSRFLALRDEIPGLVDCPKT--PKVVILTKATEYLRTLHVSDRQKAQE 383
Cdd:cd11388    3 KKWKHVEAEKKRRNQIKKGFEDLINLINYPRNNNEKriSKSELLNKAVDDIRGLLKANEQLQEE 66
bHLHzip_MGA cd18911
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and ...
323-373 7.62e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and similar proteins; MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites.


Pssm-ID: 381481  Cd Length: 65  Bit Score: 34.76  E-value: 7.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 115313792 323 RKTHNFLERKRRNDLRSRFLALRDEIpGLVDCPKTPKVVILTKATEYLRTL 373
Cdd:cd18911    1 RRTHTANERRRRNEMRDLFEKLKRTL-GLHNLPKVSKYYILKQAFEEIQGL 50
 
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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