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Conserved domains on  [gi|1723913553|gb|QEE23038|]
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tumor supressor p53, partial [Alexandromys mongolicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P53 super family cl14608
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
1-66 9.87e-25

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.


The actual alignment was detected with superfamily member cd08367:

Pssm-ID: 472693  Cd Length: 179  Bit Score: 90.02  E-value: 9.87e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1723913553   1 AMAIYKKSQHMTEVVRRCPHHERCSDGdGLAPPQHLIRVEgNLRAEYLDDRQTFRHSVVVPYEPPE 66
Cdd:cd08367    51 AMLVYKDPEHVKEPVERCPNHRQGDDG-HTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQ 114
 
Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
1-66 9.87e-25

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: 90.02  E-value: 9.87e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1723913553   1 AMAIYKKSQHMTEVVRRCPHHERCSDGdGLAPPQHLIRVEgNLRAEYLDDRQTFRHSVVVPYEPPE 66
Cdd:cd08367    51 AMLVYKDPEHVKEPVERCPNHRQGDDG-HTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQ 114
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
1-66 1.27e-19

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: 459972 [Multi-domain]  Cd Length: 191  Bit Score: 76.94  E-value: 1.27e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1723913553   1 AMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEgNLRAEYL-DDRQTFRHSVVVPYEPPE 66
Cdd:pfam00870  61 AMLVYSKSEHANDPVERCPNHRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQ 126
 
Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
1-66 9.87e-25

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: 90.02  E-value: 9.87e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1723913553   1 AMAIYKKSQHMTEVVRRCPHHERCSDGdGLAPPQHLIRVEgNLRAEYLDDRQTFRHSVVVPYEPPE 66
Cdd:cd08367    51 AMLVYKDPEHVKEPVERCPNHRQGDDG-HTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQ 114
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
1-66 1.27e-19

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: 459972 [Multi-domain]  Cd Length: 191  Bit Score: 76.94  E-value: 1.27e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1723913553   1 AMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEgNLRAEYL-DDRQTFRHSVVVPYEPPE 66
Cdd:pfam00870  61 AMLVYSKSEHANDPVERCPNHRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQ 126
 
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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