Q6LZD2
Gene name |
leuS |
Protein name |
Leucine--tRNA ligase |
Names |
Leucyl-tRNA synthetase, LeuRS |
Species |
Methanococcus maripaludis (strain S2 / LL) |
KEGG Pathway |
mmp:MMP0697 |
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 Q6LZD2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6LZD2-F1 | Predicted | AlphaFoldDB |
No variants for Q6LZD2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6LZD2 | |||||
No associated diseases with Q6LZD2
4 regional properties for Q6LZD2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 51 - 62 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 23 - 525 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 722 - 848 | IPR013155 |
| domain | Methionyl/Leucyl tRNA synthetase | 607 - 691 | IPR015413 |
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 |
| MDQKEVIGET | GHKSVDLIKI | MDKWQKKWTE | AKIFEAEHDS | RDKFFITAAF | PYLNGVLHAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HLRTFTIPET | IARYQRMKNK | NVLWTFGFHV | TGTPILGLAN | QIKERKEDII | WAYNNLHNIP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MDELLKLNTP | EAIVECFSKK | ATEAFKRMGF | SLDWRRNFKT | DDKVFSKFIE | WQFYKLKEMG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HITKGSHPVR | YCPKCENPVE | DHDLLHGEES | TTVEYSLIKF | TSKFDGKEII | MPMATLRPET |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VFGVTNAWVN | PNEIYVMAEV | HDEIQKLDSE | DVDLKYNGIW | IIGKECADKL | KEQDRKIEIL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KEIKGSELLG | LKIKNPVTKK | EVPLLPADFV | EMGIGTGCVM | SVPAHAPYDY | VALRDLGKVE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EVGLIPLIEI | EGYDKYPAKE | IVEKLGIKDQ | NDEELLEQAT | SKIYKDEFHK | GKLNENCGEY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TGISVKDIKE | KLTKDYINSN | IAEIMYEFSE | QKVVCRCGEK | CIIKTVKGQW | FINYSDENWK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KLAHECIDNM | NFAPEGIRQE | FHNKVDWMKD | KACARKRGLG | TILPFDENWI | IESLSDSTIY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MAYYTIARFI | NEGLTPEQLI | PELFDYVYLG | NGNAEEIAKN | SKIQAETIEE | MRKEFLYYYP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LDWRCSAKDL | IPNHLTFMIF | NHVALFGREH | WPRGIEINGY | VTIEGKKLSK | SKGPVLPVSE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VAENFGADVA | RFYITTCAEL | PQDADVKFKE | MEKARDNLIK | LYDLAVSVME | EESAEKELSL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IDKWLLHKTY | SSINSAETAY | EEFQLRKIGL | MFYELINDLR | WYKRRGGENN | SVLKEVVEIW |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TKLLSPVTPH | LCEEIWEKLG | YAGFISQEMY | PVSKPELINE | DLELGEEFIK | SAMEDIRNIK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| GVAKINPEKM | YLYTADDWKY | DLLEFMNENA | EKNVKALIPM | VMKEDKFKRH | GKEVMKLINE |
| 910 | 920 | 930 | 940 | 950 | |
| IMKIGVKKAI | AEVEILENAK | TFIESEFDCK | VIVNGEDVKG | KKKFAIPYKP | AIYME |