Q7MZ25
Gene name |
valS |
Protein name |
Valine--tRNA ligase |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) |
KEGG Pathway |
plu:plu4483 |
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 Q7MZ25
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7MZ25-F1 | Predicted | AlphaFoldDB |
No variants for Q7MZ25
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7MZ25 | |||||
No associated diseases with Q7MZ25
5 regional properties for Q7MZ25
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 56 - 67 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 28 - 645 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 688 - 839 | IPR013155 |
| domain | Valyl-tRNA synthetase, tRNA-binding arm | 900 - 958 | IPR019499 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 644 - 778 | 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 |
| MEKTPATQTQ | AEPSLDKTYN | PKEIEQPLYN | HWEKSGYFKP | NGDTSRESFC | IVIPPPNVTG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLHMGHAFQQ | TIMDTMIRYQ | RMQGKNTLWQ | SGTDHAGIAT | QMVVERKIAA | EEGKTRHDYG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| REAFIDKIWQ | WKAESGGTIT | NQMRRLGNSV | DWERERFTMD | EGLSNAVKEA | FVRLYQENLI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YRGKRLVNWD | PKLHTAISDL | EVENREVKGS | MWHLRYPLAD | GVTTAEGKDY | LIVATTRPET |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MLGDTGVAVN | PEDPRYKDLI | GKEIILPLIN | RRIPIIGDEH | ADMEKGTGCV | KITPAHDFND |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YEVGKRHALP | MINIMTFDGN | IRHKAEVFDT | HGEISDSYSS | DIPAEYQGIE | RFAARKTIVA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EFERLGLLVE | IKAHDLTVPY | GDRGGVVIEP | MLTDQWYVRT | APLAKVAIEA | VENGDIQFVP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KQYENMYYSW | MRDIQDWCIS | RQLWWGHRIP | AWYDTNGNVY | VGRSEEEVRR | ENNLGTDISL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NQDEDVLDTW | FSSGLWTFST | LGWPEQTDAL | KTFHPTDVLV | SGFDIIFFWI | ARMIMMTMHF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IKDENGKPQV | PFKTVYMTGL | IRDEEGQKMS | KSKGNVIDPL | DMVDGISLEE | LLEKRTGNMM |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QPQLAEKIRK | RTEKQFPAGI | ETHGTDALRF | TLAALASTGR | DINWDMKRLQ | GYRNFCNKLW |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NASRFVLMNT | EGQDCGQHGG | EMALSLADRW | ILAEFNQTVK | AYREALDTYR | FDMAANILYE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| FTWNQFCDWY | LELSKPAINK | GSEAEVRGAR | HTLIEVLEGL | LRLAHPIIPF | ITETIWQRVK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| IVKGIEADTI | MLQPFPEFAQ | EKTDELALTD | LEWIKEAIIA | VRNIRAEMNI | APGKPLEVLL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RNADAGAQRR | VAENLNFIQA | MGRLSSVTLL | STDEEAPISV | TKLINGAEVL | IPMAGLVDKE |
| 910 | 920 | 930 | 940 | 950 | 960 |
| AELSRLNKEI | EKLDKEIGAI | EGKLSNEGFV | SRAPEAVVTK | ERERLANCNT | SKEKLLAQKE |
| TIAAL |