Q5X7H7
Gene name |
tyrS |
Protein name |
Tyrosine--tRNA ligase |
Names |
Tyrosyl-tRNA synthetase, TyrRS |
Species |
Legionella pneumophila (strain Paris) |
KEGG Pathway |
lpp:lpp0628 |
EC number |
6.1.1.1: Ligases forming aminoacyl-tRNA and related compounds |
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 Q5X7H7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5X7H7-F1 | Predicted | AlphaFoldDB |
No variants for Q5X7H7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5X7H7 | |||||
No associated diseases with Q5X7H7
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.1 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| tyrosine-tRNA ligase activity | Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H(+). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tyrosyl-tRNA aminoacylation | The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase. The tyrosyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIVQDSVCSE | LMRGCEEILP | VPELEKKLQK | GIPLKIKAGF | DPTAPDLHLG | HTVLLNKLRQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FQQFGHEVIF | LIGDFTAMIG | DPTGKNVTRM | PLSQETVLEN | AKTYQHQVFK | ILDPDKTTVA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FNSQWLNKFN | AVDLIRLAAT | HTVARMLERD | DFNKRYTTGQ | PIAIHEFLYP | LLQGYDSVAL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KADVELGGTD | QKFNLLMGRE | LQKHYGFEPQ | VVMMTPLIEG | LDGVKKMSKS | LDNYIGINET |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PEQIFGKIMS | VSDELMWRYI | DLLSFKTGKE | IQQLKQSVLE | GKNPRDVKID | FAKEIVARFH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DQTQAELAHN | NFIERFQKGN | IPEDLEELSL | VIVEPIALAQ | LLKQIDLTAS | TSESIRMVKQ |
| 370 | 380 | 390 | 400 | ||
| GAVKVDGDKI | SDPSLKLPIG | KSYIIQVGKR | RIAKLSIQQA | D |