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Conserved domains on  [gi|1310961|pdb|1TUP|B]
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Protein Classification

P53 domain-containing protein (domain architecture ID 11109577)

P53 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
2-196 1.13e-133

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


:

Pssm-ID: 307150  Cd Length: 196  Bit Score: 377.66  E-value: 1.13e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B          2 SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR 81
Cdd:pfam00870   1 PTVPSTTDYPGSYGFELRFQQSGTAKSVTCTYSPDLNKLFCQLAKTCPIQVRVSTPPPPGTIVRATAVYKKSEHVAEVVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B         82 RCPHHERCSD-SDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT 160
Cdd:pfam00870  81 RCPHHERSRDfNDGLAPASHLIRVEGNQLAQYVEDPVTGRHSVVVPYEPPQVGSEFTTILYNYMCNSSCMGGMNRRPILT 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
1TUP_B        161 IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 196
Cdd:pfam00870 161 IITLETREGQLLGRRSFEVRVCACPGRDRKTEEENY 196
 
Name Accession Description Interval E-value
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
2-196 1.13e-133

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


Pssm-ID: 307150  Cd Length: 196  Bit Score: 377.66  E-value: 1.13e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B          2 SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR 81
Cdd:pfam00870   1 PTVPSTTDYPGSYGFELRFQQSGTAKSVTCTYSPDLNKLFCQLAKTCPIQVRVSTPPPPGTIVRATAVYKKSEHVAEVVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B         82 RCPHHERCSD-SDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT 160
Cdd:pfam00870  81 RCPHHERSRDfNDGLAPASHLIRVEGNQLAQYVEDPVTGRHSVVVPYEPPQVGSEFTTILYNYMCNSSCMGGMNRRPILT 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
1TUP_B        161 IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 196
Cdd:pfam00870 161 IITLETREGQLLGRRSFEVRVCACPGRDRKTEEENY 196
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
16-195 3.94e-94

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


Pssm-ID: 176262  Cd Length: 179  Bit Score: 276.46  E-value: 3.94e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B       16 FRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCsDSDGL 95
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B       96 APPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRN 175
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158
                       170       180
                ....*....|....*....|
1TUP_B      176 SFEVRVCACPGRDRRTEEEN 195
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
 
Name Accession Description Interval E-value
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
2-196 1.13e-133

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


Pssm-ID: 307150  Cd Length: 196  Bit Score: 377.66  E-value: 1.13e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B          2 SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR 81
Cdd:pfam00870   1 PTVPSTTDYPGSYGFELRFQQSGTAKSVTCTYSPDLNKLFCQLAKTCPIQVRVSTPPPPGTIVRATAVYKKSEHVAEVVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B         82 RCPHHERCSD-SDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT 160
Cdd:pfam00870  81 RCPHHERSRDfNDGLAPASHLIRVEGNQLAQYVEDPVTGRHSVVVPYEPPQVGSEFTTILYNYMCNSSCMGGMNRRPILT 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
1TUP_B        161 IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 196
Cdd:pfam00870 161 IITLETREGQLLGRRSFEVRVCACPGRDRKTEEENY 196
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
16-195 3.94e-94

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


Pssm-ID: 176262  Cd Length: 179  Bit Score: 276.46  E-value: 3.94e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B       16 FRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCsDSDGL 95
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TUP_B       96 APPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRN 175
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158
                       170       180
                ....*....|....*....|
1TUP_B      176 SFEVRVCACPGRDRRTEEEN 195
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
 
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.
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