| Analysis | rpsblast_cdd | Start | 599 |
| End | 847 | Strand | + |
| Length | 249 | Note | Gaps:20 |
| Hit Coverage | 89.69 | Hit Length | 291 |
| Hit Pident | 27.97 | E Val | 3e-47 |
| Hit Description | pfam03133 TTL Tubulin-tyrosine ligase family. Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells the tyrosinated form of tubulin predominates. However in breast cancer cells the detyrosinated form frequently predominates with a correlation to tumour aggressiveness. On the other hand 3-nitrotyrosine has been shown to be incorporated by TTL into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function including altered cell morphology epithelial barrier dysfunction and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain. | Hit Pcons | 18.01 |
| Name | Qrob_P0707870.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0707870.2 | Quercus robur | 100.0 | egn | (M=1) K16609 - tubulin--tyrosine ligase-like protein 12 | validated |
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