Q54I78
Gene name |
valS2 (DDB_G0288939) |
Protein name |
Probable valine--tRNA ligase, mitochondrial |
Names |
Valyl-tRNA synthetase, ValRS |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0288939 |
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 Q54I78
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q54I78-F1 | Predicted | AlphaFoldDB |
No variants for Q54I78
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q54I78 | |||||
No associated diseases with Q54I78
4 regional properties for Q54I78
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 71 - 82 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 44 - 683 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 743 - 909 | IPR013155 |
| domain | Valyl tRNA synthetase, anticodon-binding domain | 682 - 835 | 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNKLLFLSKK | SSTSNLYRFY | SRAPINESSI | KSSFDPKVVE | EFKYKYWQDS | GLFKPKSNNG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GEKFSMVLPP | PNVTGSLHIG | HSLTTTIQDS | LIRYNRMMGK | EVLWVPGLDH | SGIATQVAVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KELQVKQGKT | RFDLGREKFL | EQVFQWTDQY | SSNINNQLKI | TGSSLDWSRS | VFTLDEQRND |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AVQTAFIRMF | EMGLIYRSTR | LVNWCPYLQS | VISDIEVDHK | VIEKPTMLKL | KSRKKSVEVG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AIHNIAYMME | DPMLAPLIVS | TTRPETIFGD | TGLAIHPLDE | RYKDYHGKFA | IHPFNHERIP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IVLDDILVNR | EMGTGVVKIT | PAHDFNDYQC | GQRHSLPIVN | ILNSNGTLNE | NSTAEFEGVD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RLDARSMVIE | KLEQMGLYRE | KLAHPQTLSI | CSRSGDLLEP | VLKPQWYVKC | KDMADKSIEF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VESGEIKIIP | ESFRADWSRW | LTNIQDWCIS | RQLWWGNPIP | AYRVIMIDKV | TNEDLDIHLT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ETERLKQEKW | VVGKNEKEAR | ENVFKTYGIA | NAGEYRLEKD | QDVLDTWFSS | GLFPISSMGW |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PTATKNSDND | NDFSRFLPLD | VMETGSDILF | FWVARMVMMC | STLNNGEVPF | KTILLHPMIR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DSQGRKMSKS | LGNVIDPLHV | INGISLQDLK | ENLSKSNLSQ | QEKVTATKGL | EKEFPQGIPQ |
| 670 | 680 | 690 | 700 | 710 | 720 |
| CGTDSLRFSL | AQYPINGKDI | NLDISKIIGN | RLFCNKLWNA | SKFVFNYLVN | LNNLSINLYY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NNNNNEKDQQ | QPFNYLESTT | LIDKWILLKL | SKLVEIVNES | YKSNNLSIAA | QSLYSFFQYD |
| 790 | 800 | 810 | 820 | 830 | 840 |
| FCDIYIECIK | ADLSKPILSK | QNEHSSLVLA | SVLDSYLRML | HPFMPFITED | LWQRLPKSKQ |
| 850 | 860 | 870 | 880 | 890 | 900 |
| QLEIANSIEI | DDSLSIMISD | YPNPSYKYHQ | LFKNQEIEIE | KQVNLFLDTL | KLIRSQKVSL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| GINEKTKLII | KLQIIGDDQI | LIKSSFNQLK | DSFEKLLNSN | LIIDENNNND | NNNNNDNNDL |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| TNISINKFTI | SKELQISIEF | DKEINNQLNQ | KLINPNQSND | KKILKLENFI | KQLQDEIDNP |
| 1030 | 1040 | 1050 | |||
| DFKQRVPEKV | QNIKIEKLNQ | YKIELKEIYK | K |