B8FUR3
Gene name |
leuS |
Protein name |
Leucine--tRNA ligase |
Names |
Leucyl-tRNA synthetase, LeuRS |
Species |
Desulfitobacterium hafniense (strain DSM 10664 / DCB-2) |
KEGG Pathway |
dhd:Dhaf_4328 |
EC number |
6.1.1.4: 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 B8FUR3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B8FUR3-F1 | Predicted | AlphaFoldDB |
No variants for B8FUR3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B8FUR3 | |||||
No associated diseases with B8FUR3
5 regional properties for B8FUR3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 42 - 53 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 423 - 622 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 666 - 786 | IPR013155 |
| domain | Methionyl/Leucyl tRNA synthetase | 40 - 183 | IPR015413 |
| domain | Leucyl-tRNA synthetase, editing domain | 221 - 409 | IPR025709 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.4 | 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. |
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. |
| leucine-tRNA ligase activity | Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| leucyl-tRNA aminoacylation | The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-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 |
| MQEKYLFSEI | EPKWQKKWVD | RKDYQAEEHS | DKPKFYALAM | FPYPSGNLHM | GHVRNYSIVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VIARFKRMRG | YNVLHPIGWD | SFGLPAENAA | IKNQTPPAEW | TWKNIANMKR | QLQEMGISYD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WEREVTTCHP | DYYKFTQWIF | LEFYKHGLVY | KKKAGVNWCP | SCATVLANEQ | VVDGACERCD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TAVTKKDLEQ | WFFKITDYAQ | VLLDDLEKLP | GWPDKVKTMQ | KNWIGRSEGA | EVEFDLENHG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DKIRVYTTRV | DTIFGVSYVV | LAPEHPLVQK | LIAGTEYEND | VQAFIERMKG | LNEIARTSTE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TEKEGLFTGA | YCINPYSGEK | VPIWIANYVL | FEYGTGAVMG | VPAHDERDFE | FAGKYKLPIK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TVILPEGTPV | EEKDTPLQAA | FVEEGMMVNS | GEYDGLKNVE | AWEKMCDKAE | HDGFGERKVN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FRLRDWLISR | QRYWGAPIPM | IYCDHCGIVP | VPQDQLPVML | PDDVVFKAGE | NPLTTSESFK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QTICPTCGGK | ARRETDTMDT | FMCSSWYFLR | YTDPHNAQLP | FAKEAADHWM | NVDQYVGGVE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| HAILHLLYSR | FFTKALRDFG | YLKVDEPFAN | LLTQGMVCLG | GAKMSKSKGN | VVSPEEIISK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YGADTARLFI | LFAAPPERDL | EWNDQGVEGC | YRFLNRVWRL | AAQYEEVLKT | TGAGANEFGE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LDKAAKDMRR | QTHQTIQRVT | SDVGARFNFN | TAVSAIMELV | NALYLYKEQP | QVNLAVAREA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LESILILLAP | FAPHITEEIW | SELGHEDSIH | SREWPQVDEE | ALVQEEVTVV | LQINGKVKER |
| 790 | 800 | 810 | 820 | ||
| IQVPAQISAA | ELEAQVRQLP | RLGEWTQGKQ | ILKIVTVPGK | LVNVVVK |