Oalb021504.1
Basic Information
- Insect
- Odontocerum albicorne
- Gene Symbol
- -
- Assembly
- GCA_949825065.1
- Location
- OX463853.1:14234581-14235219[+]
Transcription Factor Domain
- TF Family
- P53
- Domain
- P53 domain
- PFAM
- PF00870
- TF Group
- Beta-Scaffold Factors
- Description
- 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 [PMID: 20066118, PMID: 12629332, PMID: 1397838, PMID: 6544917, PMID: 19826090, PMID: 19776744, PMID: 6278740, PMID: 221923, PMID: 6318442, PMID: 20030809].This domain is found in p53 transcription factors, where it is responsible for DNA-binding. The DNA-binding domain acts to clamp, or in the case of TonEBP, encircle the DNA target in order to stabilise the protein-DNA complex [PMID: 11780147]. Protein interactions may also serve to stabilise the protein-DNA complex, for example in the STAT-1 dimer the SH2 (Src homology 2) domain in each monomer is coupled to the DNA-binding domain to increase stability [PMID: 9630226]. The DNA-binding domain consists of a beta-sandwich formed of 9 strands in 2 sheets with a Greek-key topology. This structure is found in many transcription factors, often within the DNA-binding domain.
- Hmmscan Out
-
# of c-Evalue i-Evalue score bias hmm coord from hmm coord to ali coord from ali coord to env coord from env coord to acc 1 6 0.0026 47 4.8 0.1 55 84 29 58 21 70 0.83 2 6 0.0075 1.4e+02 3.3 0.0 60 84 58 82 56 94 0.88 3 6 0.0025 45 4.8 0.1 55 84 77 106 69 119 0.83 4 6 0.0026 48 4.7 0.2 55 84 101 130 92 142 0.83 5 6 0.0035 64 4.3 0.1 54 83 124 153 113 155 0.84 6 6 0.0019 36 5.2 0.1 54 84 148 178 137 194 0.82
Sequence Information
- Coding Sequence
- ATGCGCTTTTCCCTTTCTCGGTTGCGTCTCGCCGTTTTCACCCTCCCCTCCCCACAGCTTCGGGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCGAATTATCAGTTGCTCGAACTCCGTATCACTACAACCGAGCTCTGGCCATATATACAAGTACAACACACCGCAAATCTCGACTTAAGGCTGGACTCCATGTACCTGGTTTATGCTCCATCTTTTTATTTCGTAACTTAAGttaa
- Protein Sequence
- MRFSLSRLRLAVFTLPSPQLRELSVARTPYHYNRALAIYTSTTHRELSVARTPYHYNRALAIYTSTTHRELSVARTPYHYNRALAIYTSTTHRELSVARTPYHYNRALAIYTSTTHRELSVARTPYHYNRALAIYTSTTHRELSVARTPYHYNRALAIYTSTTHRELSVARTPYHYNRALAIYTSTTHRKSRLKAGLHVPGLCSIFLFRNLS
Similar Transcription Factors
Sequence clustering based on sequence similarity using MMseqs2
- 100% Identity
- -
- 90% Identity
- -
- 80% Identity
- -