Q9RY06
Gene name |
valS |
Protein name |
Valine--tRNA ligase |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
KEGG Pathway |
dra:DR_0148 |
EC number |
6.1.1.9: 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 Q9RY06
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9RY06-F1 | Predicted | AlphaFoldDB |
No variants for Q9RY06
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9RY06 | |||||
No associated diseases with Q9RY06
5 regional properties for Q9RY06
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 49 - 60 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 31 - 583 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 655 - 797 | IPR013155 |
| domain | Valyl-tRNA synthetase, tRNA-binding arm | 848 - 913 | IPR019499 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 584 - 742 | IPR033705 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.9 | 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 |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminoacyl-tRNA editing activity | The hydrolysis of an incorrectly aminoacylated tRNA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| valine-tRNA ligase activity | Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| valyl-tRNA aminoacylation | The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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 |
| MTDPHTTTLP | TQFDPTGIEP | KWAARWRSEP | FRADATSGKD | PFTIVIPPPN | VTGNLHLGHA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDNTLIDTLI | RYKRMAGFEA | LYLPGMDHAG | ISTQVVVERQ | LKDAGTSRHD | LGREAFLEKV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WEWKGKSGGM | ILDQLTRLGV | SADWTRERFT | MDEGLSRAVR | TQFVKLYHDG | LAYRGERIVN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WDPASQTTLS | ELEIDREVRK | GKMYTLSYKL | ENSAERGSNG | ETGEIRIATV | RPETIFADQA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IAVHPEDERF | RHLVGQKARI | PLTDRWVPII | ADEAVEMEFG | VGALKITPAH | DPTDFEVGER |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HGLERPSVID | LDGNLTRDEL | VPAEFQGLER | FAARKAVVKA | LEESGDLLEQ | KDHDTAIGLS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ERTKVPVEPI | ISEQWFVKMK | PFADQVLEGL | DKGEIKLVPE | RYTKVNRDWL | ENIRDWNISR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLWWGHQIPA | WYDKEGNIYV | PDPENPELDC | DQDPRYAHLN | LRRDPDVFDT | WFSSNLWPFS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TLGWPDTDSE | DFRKFYPTQV | LVTGYDILFF | WVARMQMAGY | GLTGQAPFST | VMLHGLYLDA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KGQKMSKSKG | NGIDPLELFG | QYGVDACRFA | FTFLSTGGQD | IKHDARRFEQ | GRNFANKLWN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ATRFALMRLG | EARIEGSDDL | SAYVRAAVTL | PDGVLLRSKD | VLAQLKERDD | LTLADRWIIS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RLNDVTAEAS | AQLDAFDIGA | AIRTLYSFTW | DEFCDWYIEA | AKPELASGNL | GTMATLKVVL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EHVLKLLHPF | MPFITSELYA | ALGHRRQIAV | HSWPQPDAAL | HDAEATKAFD | ALRSAVDSAR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SLKSELGLSP | QDRLNVAVDG | DLADVVRQNA | RVVEGIARVN | LVPALEGRTL | SQVAPGVTIL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| APLEGTVDIA | DWVKKQQKRL | AELDKQIKQA | QGKLNNEGFV | ARAPAEVIEE | EKRRVADFGA |
| 910 | |||||
| QKERLEGVLA | QLG |