O75005
Gene name |
vas2 (SPBC1709.02c, SPBC1734.18c) |
Protein name |
Valine--tRNA ligase |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC1709.02c |
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 O75005
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O75005-F1 | Predicted | AlphaFoldDB |
No variants for O75005
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O75005 | |||||
No associated diseases with O75005
4 regional properties for O75005
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 139 - 150 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 106 - 729 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 774 - 919 | IPR013155 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 728 - 865 | 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 | |
2 GO annotations of cellular component
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(+). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cytoplasmic translation | The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein. |
| cytosolic valyl-tRNA aminoacylation | The process of coupling valine to valyl-tRNA in the cytosol, catalyzed by valyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. |
| 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 |
| MADKGCEAAQ | SKDSSAPGSG | EPRPKTEKEL | ERERQKAAKL | EKYHAKLAAK | KAKEEARKPK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDKKAKIASP | VAEYVEKTTP | GEKKVLQDLD | SPALKSYNPK | AVESAWYDWW | VKSGFFEPEF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GPDGKPKKEG | VFVITSPPPN | VTGALHIGHA | LTIAIQDSLA | RWNRMLGKTV | LFLGGFDHAG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LSTQSVVEKK | LWYTQKKTRH | DYPRDKFVDI | VWEWKEEYHN | RIKNQMSRLG | GSFDWTREAF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TMDENLSRAV | VETFVRLHEE | NIIYRANRLV | NWCTALQTTL | SNLEVENVDV | PGRTLLKVPG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YDEPVEVGVL | TSIAYAVEGS | DERIVIATTR | PETLLGDTAV | AVHPQDPRYK | HLHGKFVKHP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FCNRSIPIIC | DDIIVDMEFG | TGAVKITPAH | DPNDYEVGKR | HNLEFINIFT | DDGLLNENCG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EFAGMKRFTA | RVKVVERLKE | LGLFVGTKEN | PMVIPLCGKT | SDIIEPVMKP | QWWVNQKEMA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AAAAEVVKSG | EIEIAPDMSR | REFIRWMENI | QDWCISRQLW | WGHRIPAYFV | NLADEPSQDR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SEGRYWVTGR | TLEQAEEKAK | AAFPGKSFTL | EQDEDVLDTW | FSSGLWPFST | LGWPKDTSDY |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ENFYPTTLME | TGWDILFFWI | ARMVMLGLKL | TGKIPFKRVF | CHALVRDAQG | RKMSKSLGNV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VDPIDVIEGI | SLQALHDKLL | VGNLDSREVE | KAKKGQRLSY | PKGIPQCGTD | ALRFTLCSLT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| TGGRDLNLDI | LRVEGYRKFC | NKLYNATKFA | LGRLGSNFVP | NKTADLTGNE | SLVEKWIFHR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LNIAAAAMNK | NMEEMNFLQA | TSAVHQFWLY | ELCDVYIENS | KYLLSDGTEV | QQESAKQTLY |
| 850 | 860 | 870 | 880 | 890 | 900 |
| TVLDNALRLM | HPFMPYVTEE | MWQRLPRRPG | DKTQTIVKAA | FPVERVDYSN | EIAAKYYESI |
| 910 | 920 | 930 | 940 | 950 | 960 |
| ITVVHSTRSM | MAENGIKSDA | VVYIHPDEEH | SKLITSESAS | IQSLIKKCKT | LSIVDNTFDS |
| 970 | |||||
| DKCVKNEVLE | GSTIFLERNN |