Q5TM74
Gene name |
VARS2 |
Protein name |
Valine--tRNA ligase, mitochondrial |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Macaca mulatta (Rhesus macaque) |
KEGG Pathway |
|
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 Q5TM74
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5TM74-F1 | Predicted | AlphaFoldDB |
No variants for Q5TM74
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5TM74 | |||||
No associated diseases with Q5TM74
4 regional properties for Q5TM74
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 146 - 157 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 113 - 730 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 780 - 928 | IPR013155 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 735 - 869 | 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
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
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. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P07118 | valS | Valine--tRNA ligase | Escherichia coli (strain K12) | PR |
| P26640 | VARS1 | Valine--tRNA ligase | Homo sapiens (Human) | PR |
| Q5ST30 | VARS2 | Valine--tRNA ligase, mitochondrial | Homo sapiens (Human) | PR |
| Q9Z1Q9 | Vars1 | Valine--tRNA ligase | Mus musculus (Mouse) | PR |
| Q04462 | Vars1 | Valine--tRNA ligase | Rattus norvegicus (Rat) | PR |
| Q9U1Q4 | glp-4 | Valine--tRNA ligase | Caenorhabditis elegans | PR |
| P93736 | TWN2 | Valine--tRNA ligase, mitochondrial 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPHLPLASFR | PPFWGLRHSR | GLPRFHSVST | QSEPHGSPIS | RRNREAKQKR | LREKQATLET |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DIAGESKSPA | ESIKAWSPKE | VVLYEIPTKP | GEKKDVSGPL | PPAYSPRYVE | AAWYPWWVRE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GFFKPEYQAR | LPQATGETFS | MCIPPPNVTG | SLHIGHALTV | AIQDALVRWH | RMRGDQVLWV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PGSDHAGIAT | QAVVEKQLWK | EQGVRRHELS | REAFLREVWQ | WKEAKGGEIC | EQLRALGASL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DWDRECFTMD | VGSSVAVTEA | FVRLYKAGLL | YRNRRLGRWM | SCPLTQLSRR | FQVENRPLPG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RTQLRLPGCP | TPVSFGLLFS | VAFPVDGEPD | AEVVVGTTRP | ETLPGDVAVA | VHPDDSRYTH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LHGRQLRHPL | MGQPLPLITD | YAVQPHVGTG | AVKVTPAHSP | ADAEMGARHG | LSPLNVIAED |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GTMTSLCGDW | LQGLHRFVAR | EKIVSVLSER | GLFRGLQNHP | MVLPICSRSG | DVIEYLLKSQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WFVRCQEMGA | RAAQAVESGA | LELSPSFHQK | NWQHWFSHIG | DWCVSRQLWW | GHQIPAYLVV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EDHAQGEEDC | WVVGRSEAEA | REVAAELTGR | PGAELALERD | PDVLDTWFSS | ALFPFSALGW |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PQETPDLARF | YPLSLLETGS | DLLLFWVGRM | VMLGTQLTGR | LPFSKVLLHP | MVRDRQGRKM |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SKSLGNVLDP | RHIISGAEMQ | VLQEKLRSGN | LDPAELAIVA | AAQKKDFPHG | IPECGTDALR |
| 730 | 740 | 750 | 760 | 770 | 780 |
| FTLCSHGVQG | GDLCLSVSEV | QSCRHFCNKI | WNALRFILNA | LGEKFVPQPA | KELSPSCHMD |
| 790 | 800 | 810 | 820 | 830 | 840 |
| AWILSRLALT | ARECERGFLT | RELSLVTHAL | HHFWLHNLCD | VYLEAVKPVL | RHSPCPPGPP |
| 850 | 860 | 870 | 880 | 890 | 900 |
| QVLFSCADIG | LRLLAPLMPF | LAEELWQRLP | PRPGCPPAPS | ISVAPYPSPC | SLEHWRQPEL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| ERRFSRVQEV | VQVLRALRAT | YQLTKARPRV | LLQSSEPGDQ | GLFEAFLEPL | GTLSHCGAVG |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| LLPPGAAAPS | GWAQAPLSDT | VQVYMELQGL | VDPQIQLPLL | AARRSKLQKQ | LDGLMARTPS |
| 1030 | 1040 | 1050 | 1060 | ||
| EGEAGTQRQQ | RLSSLQLELS | KLDKAASHLR | QLMDEPPAPG | SPEL |