A1TRL4
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp citrulli) |
KEGG Pathway |
aav:Aave_3035 |
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 A1TRL4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1TRL4-F1 | Predicted | AlphaFoldDB |
No variants for A1TRL4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1TRL4 | |||||
No associated diseases with A1TRL4
5 regional properties for A1TRL4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DHHA1 domain | 809 - 944 | IPR003156 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 727 - 769 | IPR012947 |
| domain | Alanyl-tRNA synthetase, class IIc, N-terminal | 12 - 398 | IPR018164-1 |
| domain | Alanyl-tRNA synthetase, class IIc, N-terminal | 450 - 628 | IPR018164-2 |
| domain | Alanyl-tRNA synthetase, class IIc, core domain | 8 - 782 | IPR018165 |
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 |
| MTKPTPPSSV | ADIRKSFLDF | FASKGHTVVP | SSPLVPGNDP | TLMFTNSGMV | QFKDVFLGTD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KRPYVRATSV | QACLRAGGKH | NDLENVGYTA | RHHTFFEMLG | NWSFGDYFKR | DSLKWAWELL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TEVYGLPKER | LLATVYAEDD | EAYDIWTKEI | GLPPERVIRI | GDNKGGRYKS | DNFWMMADTG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PCGPCSEIFY | DHGPHIPGGP | PGSPDEDGDR | FIEIWNNVFM | QFDMAEDGSV | TPLPAPCVDT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GMGLERLAAI | LQHVHSNYEI | DLFAALIQAA | ARETGTADLA | NPSLKVIADH | IRATAFLVSD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GVIPSNEGRG | YVQRRIVRRA | IRHGYKLGRK | TPFFHSLVKD | LVAQMGDAYP | KLREQEQRIT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EVLKAEEERF | FETLANGMDL | LDSALDIQLA | SKALQNKTLR | WFASEGREEK | LVSFKDDVQV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AEAVLISDEL | RSTEYMQRLK | ETVPGLNEVK | TLHSVIRDWS | GLTLPGDLAF | KLHDTYGFPL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DLTNDVCRER | GVTVDEDGFK | AAMDRQKAQA | RAAGKFKMDK | ALEYGGEANR | FSGYDGLTES |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AKIVAIYVDG | TSAQALEAGQ | NGVVVLDNTP | FYAESGGQVG | DQGVIHAGGA | RFAVDDTLKI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RADVYGHHGR | LESGTLRVGD | AVQAEVDAAL | RAATMRNHSV | THIMHKALRE | VLGSHVQQKG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SLVNAERTRF | DFAHNAPVTD | AQIREIERRV | NEEILANTPT | GARVMDIESA | QKTGAMMLFG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EKYGETVRVL | DIGTSRELCG | GTHVARTGDI | GLFKVVGESG | VAAGVRRIEA | VTGAGALAYL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| QQLEDTVAKA | AGALRAPAAE | ITGRIGQALE | QVKALEREVA | ALKGKLASSQ | GDELAGQAVD |
| 850 | 860 | 870 | 880 | 890 | 900 |
| VKGLKVLAAT | LPGADAKTLR | DTMDKLKDKL | KSAAIVLAAV | DGAKVQIAAG | VTPDAMAKVK |
| 910 | 920 | 930 | 940 | ||
| AGELVNFVAS | QVGGKGGGKP | DMAMAGGTDA | AALPAALASV | AAWVGERA |