P9WFV3
Gene name |
ileS (Rv1536, MTCY48.29c) |
Protein name |
Isoleucine--tRNA ligase |
Names |
Isoleucyl-tRNA synthetase, IleRS |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv1536 |
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 P9WFV3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P9WFV3-F1 | Predicted | AlphaFoldDB |
No variants for P9WFV3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WFV3 | |||||
No associated diseases with P9WFV3
4 regional properties for P9WFV3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 53 - 64 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 23 - 653 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 701 - 840 | IPR013155 |
| domain | Isoleucyl tRNA synthetase type 2, anticodon-binding domain | 659 - 825 | IPR033709 |
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 | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| peptidoglycan-based cell wall | A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
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). |
2 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. |
| response to antibiotic | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDNAYPKLA | GGAPDLPALE | LEVLDYWSRD | DTFRASIARR | DGAPEYVFYD | GPPFANGLPH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YGHLLTGYVK | DIVPRYRTMR | GYKVERRFGW | DTHGLPAELE | VERQLGITDK | SQIEAMGIAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FNDACRASVL | RYTDEWQAYV | TRQARWVDFD | NDYKTLDLAY | MESVIWAFKQ | LWDKGLAYEG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YRVLPYCWRD | ETPLSNHELR | MDDDVYQSRQ | DPAVTVGFKV | VGGQPDNGLD | GAYLLVWTTT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PWTLPSNLAV | AVSPDITYVQ | VQAGDRRFVL | AEARLAAYAR | ELGEEPVVLG | TYRGAELLGT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RYLPPFAYFM | DWPNAFQVLA | GDFVTTDDGT | GIVHMAPAYG | EDDMVVAEAV | GIAPVTPVDS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KGRFDVTVAD | YQGQHVFDAN | AQIVRDLKTQ | SGPAAVNGPV | LIRHETYEHP | YPHCWRCRNP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LIYRSVSSWF | VRVTDFRDRM | VELNQQITWY | PEHVKDGQFG | KWLQGARDWS | ISRNRYWGTP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IPVWKSDDPA | YPRIDVYGSL | DELERDFGVR | PANLHRPYID | ELTRPNPDDP | TGRSTMRRIP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DVLDVWFDSG | SMPYAQVHYP | FENLDWFQGH | YPGDFIVEYI | GQTRGWFYTL | HVLATALFDR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PAFKTCVAHG | IVLGFDGQKM | SKSLRNYPDV | TEVFDRDGSD | AMRWFLMASP | ILRGGNLIVT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EQGIRDGVRQ | VLLPLWNTYS | FLALYAPKVG | TWRVDSVHVL | DRYILAKLAV | LRDDLSESME |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VYDIPGACEH | LRQFTEALTN | WYVRRSRSRF | WAEDADAIDT | LHTVLEVTTR | LAAPLLPLIT |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EIIWRGLTRE | RSVHLTDWPA | PDLLPSDADL | VAAMDQVRDV | CSAASSLRKA | KKLRVRLPLP |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KLIVAVENPQ | LLRPFVDLIG | DELNVKQVEL | TDAIDTYGRF | ELTVNARVAG | PRLGKDVQAA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| IKAVKAGDGV | INPDGTLLAG | PAVLTPDEYN | SRLVAADPES | TAALPDGAGL | VVLDGTVTAE |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| LEAEGWAKDR | IRELQELRKS | TGLDVSDRIR | VVMSVPAERE | DWARTHRDLI | AGEILATDFE |
| 1030 | 1040 | ||||
| FADLADGVAI | GDGVRVSIEK | T |