NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|297265466|ref|XP_001091369|]
View 

PREDICTED: N-myc proto-oncogene protein isoform X2 [Macaca mulatta]

Protein Classification

Myc_N and HLH domain-containing protein (domain architecture ID 10470923)

Myc_N and HLH domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

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 ...
101-463 2.83e-170

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: 307275  Cd Length: 329  Bit Score: 489.71  E-value: 2.83e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  101 PGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWG 180
Cdd:pfam01056   1 PGMICKNYDLEFDSLQPCFYPDEDDFYFGGPQSTPPGEDIWKKFELLPTPPLSPSRRGSESTADPLEWATEMLLPADLWN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  181 SPAEEDAFglgglggltPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAG 260
Cdd:pfam01056  81 DPDEEDSF---------LKSIIIQDCMWSGFSAAEKLEKVVSEKLASGQAARKEGAATPAPGAGAASPAGRARSGSAGAG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  261 RAGAALPAELAHPAAECVDPAVVFPFPVNKREpapmpaapasapavgpavasgagvSAPAGAPGVAPPRPGGRQTNGGDH 340
Cdd:pfam01056 152 RSSAAYLQDLSHSASECVDPAVVFPFPLNKRE------------------------KAATVTPPNTIPASGGSPSSSSDS 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  341 KALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQ 420
Cdd:pfam01056 208 KALSSSGEDTLSDSDDEEEEEEDEEEEIDVVTVEKRQSSSKRKEVTTLTITVRPKNTALGPSRAQSSELILKRCHVIHHQ 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 297265466  421 HNYAAPSPYVESEDAPPQKKIKNEVSPRPLKSVIpPKAKSLSP 463
Cdd:pfam01056 288 HNYAAPSPYTESEDAPPQKKLKLESSPRPLKQIS-PKRKCSSP 329
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
470-529 2.74e-18

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


:

Pssm-ID: 238036  Cd Length: 60  Bit Score: 80.72  E-value: 2.74e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466 470 DSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEH 529
Cdd:cd00083    1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPPSKKLSKAEILRKAVDYIKSLQELLQ 60
 
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 ...
101-463 2.83e-170

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: 307275  Cd Length: 329  Bit Score: 489.71  E-value: 2.83e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  101 PGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWG 180
Cdd:pfam01056   1 PGMICKNYDLEFDSLQPCFYPDEDDFYFGGPQSTPPGEDIWKKFELLPTPPLSPSRRGSESTADPLEWATEMLLPADLWN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  181 SPAEEDAFglgglggltPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAG 260
Cdd:pfam01056  81 DPDEEDSF---------LKSIIIQDCMWSGFSAAEKLEKVVSEKLASGQAARKEGAATPAPGAGAASPAGRARSGSAGAG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  261 RAGAALPAELAHPAAECVDPAVVFPFPVNKREpapmpaapasapavgpavasgagvSAPAGAPGVAPPRPGGRQTNGGDH 340
Cdd:pfam01056 152 RSSAAYLQDLSHSASECVDPAVVFPFPLNKRE------------------------KAATVTPPNTIPASGGSPSSSSDS 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  341 KALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQ 420
Cdd:pfam01056 208 KALSSSGEDTLSDSDDEEEEEEDEEEEIDVVTVEKRQSSSKRKEVTTLTITVRPKNTALGPSRAQSSELILKRCHVIHHQ 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 297265466  421 HNYAAPSPYVESEDAPPQKKIKNEVSPRPLKSVIpPKAKSLSP 463
Cdd:pfam01056 288 HNYAAPSPYTESEDAPPQKKLKLESSPRPLKQIS-PKRKCSSP 329
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
470-529 2.74e-18

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 80.72  E-value: 2.74e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466 470 DSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEH 529
Cdd:cd00083    1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPPSKKLSKAEILRKAVDYIKSLQELLQ 60
HLH pfam00010
Helix-loop-helix DNA-binding domain;
473-525 2.75e-15

Helix-loop-helix DNA-binding domain;


Pssm-ID: 306515  Cd Length: 52  Bit Score: 71.80  E-value: 2.75e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 297265466  473 RRRNHNILERQRRNDLRSSFLTLRDHVPELvKNEKAAKVVILKKATEYVHSLQ 525
Cdd:pfam00010   1 RRRAHNERERRRRDRINDAFDELRELLPTP-PSKKLSKAEILRLAIEYIKHLQ 52
HLH smart00353
helix loop helix domain;
478-530 2.84e-15

helix loop helix domain;


Pssm-ID: 197674  Cd Length: 53  Bit Score: 71.87  E-value: 2.84e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 297265466   478 NILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQ 530
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
 
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 ...
101-463 2.83e-170

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: 307275  Cd Length: 329  Bit Score: 489.71  E-value: 2.83e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  101 PGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWG 180
Cdd:pfam01056   1 PGMICKNYDLEFDSLQPCFYPDEDDFYFGGPQSTPPGEDIWKKFELLPTPPLSPSRRGSESTADPLEWATEMLLPADLWN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  181 SPAEEDAFglgglggltPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAG 260
Cdd:pfam01056  81 DPDEEDSF---------LKSIIIQDCMWSGFSAAEKLEKVVSEKLASGQAARKEGAATPAPGAGAASPAGRARSGSAGAG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  261 RAGAALPAELAHPAAECVDPAVVFPFPVNKREpapmpaapasapavgpavasgagvSAPAGAPGVAPPRPGGRQTNGGDH 340
Cdd:pfam01056 152 RSSAAYLQDLSHSASECVDPAVVFPFPLNKRE------------------------KAATVTPPNTIPASGGSPSSSSDS 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466  341 KALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQ 420
Cdd:pfam01056 208 KALSSSGEDTLSDSDDEEEEEEDEEEEIDVVTVEKRQSSSKRKEVTTLTITVRPKNTALGPSRAQSSELILKRCHVIHHQ 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 297265466  421 HNYAAPSPYVESEDAPPQKKIKNEVSPRPLKSVIpPKAKSLSP 463
Cdd:pfam01056 288 HNYAAPSPYTESEDAPPQKKLKLESSPRPLKQIS-PKRKCSSP 329
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
470-529 2.74e-18

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 80.72  E-value: 2.74e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265466 470 DSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEH 529
Cdd:cd00083    1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPPSKKLSKAEILRKAVDYIKSLQELLQ 60
HLH pfam00010
Helix-loop-helix DNA-binding domain;
473-525 2.75e-15

Helix-loop-helix DNA-binding domain;


Pssm-ID: 306515  Cd Length: 52  Bit Score: 71.80  E-value: 2.75e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 297265466  473 RRRNHNILERQRRNDLRSSFLTLRDHVPELvKNEKAAKVVILKKATEYVHSLQ 525
Cdd:pfam00010   1 RRRAHNERERRRRDRINDAFDELRELLPTP-PSKKLSKAEILRLAIEYIKHLQ 52
HLH smart00353
helix loop helix domain;
478-530 2.84e-15

helix loop helix domain;


Pssm-ID: 197674  Cd Length: 53  Bit Score: 71.87  E-value: 2.84e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 297265466   478 NILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQ 530
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH