B5Y1P2
Gene name |
gluQ |
Protein name |
Glutamyl-Q tRNA(Asp) synthetase |
Names |
Glu-Q-RSs |
Species |
Klebsiella pneumoniae (strain 342) |
KEGG Pathway |
kpe:KPK_4592 |
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 B5Y1P2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B5Y1P2-F1 | Predicted | AlphaFoldDB |
No variants for B5Y1P2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B5Y1P2 | |||||
No associated diseases with B5Y1P2
1 regional properties for B5Y1P2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain | 9 - 277 | IPR020058 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminoacyl-tRNA ligase activity | Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glutamyl-tRNA aminoacylation | The process of coupling glutamate to glutamyl-tRNA, catalyzed by glutamyl-tRNA synthetase. The glutamyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamic acid-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
| 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 |
| MTDSRYIGRF | APSPSGELHF | GSLIAALGSY | LQARANQGIW | RVRIEDIDPP | REVPGAADTI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LRQLDHYGLH | WDGDVLWQSQ | RHEAYREALA | WLGEQGLSYY | CTCTRARIHA | VGGIYDGHCR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DLGLGAENAA | LRLRQTRPVL | QFTDRLHGTL | IANEPLARED | FIIHRRDGLF | AYNLAVVVDD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HFQGITEIVR | GADLIEPTVR | QISLYQHFGW | QAPDYLHLPL | ALNADGNKLS | KQNHAPALPE |
| 250 | 260 | 270 | 280 | 290 | |
| GDPRPEIVRA | LRFLNQDIAQ | DWQALSMDDL | LSQAVANWQP | AKIEHSQMAP | AEL |