A1WIG8
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Verminephrobacter eiseniae (strain EF01-2) |
KEGG Pathway |
vei:Veis_1670 |
EC number |
6.1.1.7: 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 A1WIG8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1WIG8-F1 | Predicted | AlphaFoldDB |
No variants for A1WIG8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1WIG8 | |||||
No associated diseases with A1WIG8
4 regional properties for A1WIG8
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.7 | 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| alanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| alanyl-tRNA aminoacylation | The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPSISVADIR | KSFLDFFVAK | GHTIVASSPL | VPGNDPTLMF | TNSGMVQFKD | VFLGTDKRPY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SRAVSVQACL | RAGGKHNDLE | NVGYTARHHT | FFEMLGNWSF | GDYFKRESLQ | WAWELLTEVY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RLPAERLLAT | VYQDDDEAYD | IWTREIGLPP | ERVIRIGDNK | GGRYKSDNFW | MMADTGPCGP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CSEIFYDHGP | GIPGGPPGSP | DEDGDRFIEI | WNNVFMQFNM | AADGSVTPLP | APCVDTGMGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ERLAAVLQQV | HSNYEIDLFE | QLIAAASRET | GEKDLGHKSL | RVIADHIRAS | AFLVSDGVLP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GSEGRGYVQR | RIMRRAIRHG | YQLGQRAPFL | HRLVADLVRL | MGAAYPSLRA | QQQRIADILK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AEEERFFETL | AHGMEILDAA | LDGGAKLLPG | DVAFKLHDTY | GFPLDLSADM | CRERGVAVDE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AGFHLAMERQ | KTQARAAGKF | KMERALEYTG | GASRFTGYED | LAGTAKITAI | YAAGTSVAAL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KTGQHGVLVL | DRTPFYAESG | GQVGDQGLIS | SGSARFAVDD | TLKIKADVHG | HHGRLEDGTL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NVGDTVQARV | NTALRAATMR | NHSATHLMHQ | ALRAVLGSHV | QQKGSLVNAE | RTRFDFAHNA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AVSSAELREI | ERRVNEEILA | NQPTQARVMD | IEAARSSGAM | MLFDEKYGAA | VRVLDIGSSR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ELCAGTHVQR | TGDIGLFKVV | AEGGVAAGVR | RIEAVTGSHA | LAWLQQLEDT | VNQAADTLRA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PVAELNGRIS | QALDNARALE | KEVAALKSRL | AASQGQELLA | RAVQIKGLAV | LAATLPGADA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| KTLRATMDQL | KDQLKTAAIV | LAAVDGDKVQ | LAAGVTADSV | GRIQAGDLVN | FVARQVGGKG |
| 850 | 860 | 870 | |||
| GGKPDMAMAG | GTDAAGLPAA | LASVAGWVSG | RL |