Q65EW5
Gene name |
trhO |
Protein name |
tRNA uridine(34) hydroxylase |
Names |
tRNA hydroxylation protein O |
Species |
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) |
KEGG Pathway |
bli:BL00834 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q65EW5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q65EW5-F1 | Predicted | AlphaFoldDB |
No variants for Q65EW5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q65EW5 | |||||
No associated diseases with Q65EW5
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tRNA modification | The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKNQYRVLLY | YKYVHIDNPE | QFAEDHLKFC | KDLGLKGRIL | VAGEGINGTV | SGTVEQTDRY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MSEMKSDPRF | EDMVFKIDES | EGHAFKKMHV | RHRDELVTLR | LEDDIDPNEL | TGKYLEPKEF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YEAMQQEDTI | VVDARNDYEY | DLGHFRGAIR | PDIKAFRELP | EWIRDNKEKL | EGKKILTYCT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GGIRCEKFSG | WLKKEGFEDV | SQLHGGIVTY | GKDPEVQGEL | WDGKCYVFDE | RISVPVNQKE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HVIVGKDYFT | GEPCERYVNC | ANPECNKQII | CSEENEHRYL | RGCTHECRVH | PRNLYVKEHG |
| 310 | 320 | ||||
| LSEEEVQERL | EKLKEEEHAA | QS |