Q8FN65
Gene name |
valS |
Protein name |
Valine--tRNA ligase |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) |
KEGG Pathway |
cef:CE2282 |
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 Q8FN65
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8FN65-F1 | Predicted | AlphaFoldDB |
No variants for Q8FN65
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8FN65 | |||||
No associated diseases with Q8FN65
6 regional properties for Q8FN65
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 61 - 72 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 33 - 446 | IPR002300-1 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 454 - 586 | IPR002300-2 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 633 - 782 | IPR013155 |
| domain | Valyl-tRNA synthetase, tRNA-binding arm | 838 - 903 | IPR019499 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 593 - 725 | 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 |
| MVCVTDQNNE | NPSQNRADKL | PKSWDPKAVE | ADLYQGWVDA | GYFTADPASE | KPGYSIVLPP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNVTGQLHMG | HALDHTLMDA | LARRKRMQGF | EVLWLPGMDH | AGIATQTKVE | EMLKETEGKS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RYDYSREEFI | EKVWEWKKEY | GGKIGEQMRA | IGDSVDWSRE | RFTLDEGLSR | AVQTIFKKLY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DSGMIYQANR | LVNWSPVLET | AVSDIEVVYK | DVEGELVSIR | YGSLNDDEPH | VVVATTRVET |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MLGDVAVAVH | PDDERYRHLV | GTTLPHPFRD | DLTLKVVADD | YVDPEFGSGA | VKITPAHDPN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DYALGLRHHL | DMPTIMDKTG | RIADTGTQFD | GMTREEARVK | VREALAEQGR | IVKEVRPYVH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SVGHSERSGE | AIEPRLSLQW | WVKVEELAKM | SGDAVRAGDT | TIHPKSLEPR | YFDWVDDMHD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WCISRQLWWG | HRIPIWYGPD | GDVICVGPDE | QAPEGYTQDP | DVLDTWFSSA | LWPFSTMGWP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DKTPELDKFY | PTSVLVTAYD | ILFFWVARMM | MFGTFAAKET | PELLGEGTDG | RPQVPFTDLF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LHGLVRDEHG | RKMSKSLGNG | IDPMDWVDNY | GADALRFTLA | RGANPGVDLP | VGEDSAQSSR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NFATKLFNAT | RFALMNGAVS | EGLPERAELT | DADRWILDRL | EEVRGHVDDY | LDNYQFAKAN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EELYHFAWNE | FCDWYLEIAK | VQIPREGVTE | RGRNTQQVLG | HVLDALLRLL | HPAMPFVTEV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LWKALTDGES | IVTSSWPTPA | DTNGGAAVDA | DAARRIADVE | KLVTEIRRFR | SDQGVKPSQK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| VPARLDFAAC | DLTELEGAVR | ALVRIEEPAE | DFEESASLEI | RLSTATITVE | LDTSGTVDVA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| AERKRLEKDL | ATANKELETT | GKKLGNEAFL | AKAPDAVVEK | IRGRQQVARE | EVERITKRLE |
| ELG |