Q493Z9
Gene name |
valS |
Protein name |
Valine--tRNA ligase |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Blochmannia pennsylvanicus (strain BPEN) |
KEGG Pathway |
bpn:BPEN_033 |
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 Q493Z9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q493Z9-F1 | Predicted | AlphaFoldDB |
No variants for Q493Z9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q493Z9 | |||||
No associated diseases with Q493Z9
4 regional properties for Q493Z9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 47 - 58 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 19 - 635 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 680 - 831 | IPR013155 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 634 - 769 | 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 |
|---|---|
| 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 |
|---|---|
| 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 |
| MSNYIVEKIY | NPKNIEEPIY | KFWEYGDYFS | PHGNTSQESY | CIMMPPPNIT | GQLHLGHAFQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QTIMDVLIRY | QRMQGKNTLW | QTGTDHAGIA | TQMLVEHKIY | NNTGKTRHDY | TRDELIKNIW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AWKSQSEQFI | TYQMKRLGNS | VDWKRQRFTM | DTEMSYAVTE | AFIRLYRKNL | IYRGKRLVNW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DCKLQTAISD | LEVINKKTKG | SIWYIYYKLD | NATISSNSHH | LIVATTRPET | MLGDTAVAVH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PEDTRYKNYI | GQYVIAPITN | RRIPIISDKN | VDMFKGTGCL | KITPAHDFND | YIIGKRHGLP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MINIFSLNGK | ILKKLEVFNS | SGQLTDQLYC | KIPQIFHNLD | SDNARKKIIS | ECNALKLLHN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IEPHDLTIPY | SDRTGTIIEP | MLTDQWYIRV | KHLTQHAIDA | VNLNIINFVP | KQYKNMYFSW |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MNNLQDWCIS | RQIWWGHKIP | AWYDDNNTIY | VGYCEKDIRI | KNKLNNNVIL | HREKDVLDTW |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FSSSLWTFAA | LGWPKNTNLL | NVFHPTNIII | SGFDIIFFWI | ARMIMLTMHF | IKNDNGSAQI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PFKTVYITGL | IRDELGQKMS | KSKGNIIDPI | DIIDGISIEN | LLKKRTKNML | QPQLSKHIIN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NTIKQFPNGI | KPHGTDALRF | TLVALASSGR | DIHWDMQRLT | GYRNFCNKLW | HASRFVLMHT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KNQDCGISIN | INEKSFSLAD | RWIITKFHQT | VQIFHKKLEI | YRFDEIANIL | HEFIWHQFCD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| WYLELTKPIL | YHGNALELRG | TRYTLITLLE | SLLRLTHPII | PFITEKIWQE | VKTVTGNNGT |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TIMLQPFPKY | DESVIDMKSV | IDIEWIKNAV | LAIRTARVNM | NISYNIPLQI | VFRDTSSEVK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KRITENSKIL | CHIAQLKSIH | FISKGTIYPK | SMTMPLDSSE | LLIRIPDTFN | KENEINRLKK |
| 910 | 920 | 930 | 940 | 950 | |
| ESELINRKIE | TIQKLLDDNN | FINQAPKSVI | KDKQALLNYY | ELIQNKLIDQ | CAIMKKL |