Q2RK59
Gene name |
ileS |
Protein name |
Isoleucine--tRNA ligase |
Names |
Isoleucyl-tRNA synthetase, IleRS |
Species |
Moorella thermoacetica (strain ATCC 39073 / JCM 9320) |
KEGG Pathway |
mta:Moth_0863 |
EC number |
6.1.1.5: 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 Q2RK59
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2RK59-F1 | Predicted | AlphaFoldDB |
No variants for Q2RK59
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2RK59 | |||||
No associated diseases with Q2RK59
5 regional properties for Q2RK59
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 58 - 69 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 28 - 647 | IPR002300 |
| domain | Zinc finger, FPG/IleRS-type | 890 - 917 | IPR010663 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 692 - 845 | IPR013155 |
| domain | Isoleucyl tRNA synthetase type 1, anticodon-binding domain | 647 - 823 | IPR033708 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.5 | 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. |
5 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. |
| isoleucine-tRNA ligase activity | Catalysis of the reaction: L-isoleucine + ATP + tRNA(Ile) = L-isoleucyl-tRNA(Ile) + AMP + diphosphate + 2 H(+). |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| isoleucyl-tRNA aminoacylation | The process of coupling isoleucine to isoleucyl-tRNA, catalyzed by isoleucyl-tRNA synthetase. The isoleucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a isoleucine-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 |
| MDYSKTLNLP | RTDFPMRANL | PQREPEILKF | WEENDIYGKV | QEANRGKPKF | ILHDGPPYAN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GHLHLGHTLN | KILKDIIIKY | HSMNGYDAPY | VPGWDTHGLP | IEQQAIKNLG | LNRHAVDVVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FRNRCRDYAL | KYVNIQREEF | KRLGVRGDWE | HPYLTLEPEY | EAIQIGIFGE | MAKKGYIYKG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKPVYWCTDC | ETALAEAEVE | YGEERSPSIY | VKFPVADARG | LFEPRGSSIV | IWTTTPWTLP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ANVAIALHPE | FKYVLIQVGE | ERLLMAAELV | RPVLELLGVK | DYQVVATFTG | SELEGVVCRN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLMDRDSVVI | LGEHVTLEQG | TGCVHTAPGH | GLEDYEVGMR | YHLPVLSPLD | DRGRFTEEGG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QFAGLFIDEA | NKAVVKELEA | RGALLHFGFI | KHQYPHCWRC | KHPIIFRATE | QWFASIEGFR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QEALEAIKKV | KWIPSWGEDR | IYNMVADRSD | WCISRQRTWG | VPIPIFYCAN | CGREIINDAT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ISHLQELFRK | HGSNVWFARE | AGELVPPGLK | CPECGSKEFR | KETDIMDVWF | DSGSSHAAVL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ATRPELAWPA | DLYLEGSDQH | RGWFNSSLST | AVATRGRAPY | RQVLTHGFLV | DEEGRKMSKS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LGNGIDPADV | IRQRGADVLR | LWVASADYRR | DVAASENIMR | QITEAYRKIR | NTCRFLLANL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ADFDPGKDQV | PREEMLELDR | WAMNRLQRLI | ARVTMAYDDY | EFHVVYHTIH | NFCAVDLSAV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YLDIIKDRLY | TWPAASKGRR | SAQTVLYETI | NVLVRLLTPI | LAFTTEEIWR | YLPGEDDRPI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SVQLAGWPQV | KTEFLDDELE | EKWKRILQVR | DVVARALERA | RQEQDLGNSL | NAAVHLYPDA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| DMYQFLKPLG | DELATIMIVS | RVDLHQPGEE | APAGSLEAPE | LPGLRVYVTG | APGQKCERCW |
| 910 | 920 | ||||
| MVSETVGQDT | DHPTLCRRCA | TVVKEMYMNG |