Q65RQ2
Gene name |
ileS |
Protein name |
Isoleucine--tRNA ligase |
Names |
Isoleucyl-tRNA synthetase, IleRS |
Species |
Mannheimia succiniciproducens (strain MBEL55E) |
KEGG Pathway |
msu:MS1751 |
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 Q65RQ2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q65RQ2-F1 | Predicted | AlphaFoldDB |
No variants for Q65RQ2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q65RQ2 | |||||
No associated diseases with Q65RQ2
4 regional properties for Q65RQ2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 65 - 76 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 35 - 647 | IPR002300 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 692 - 849 | IPR013155 |
| domain | Isoleucyl tRNA synthetase type 1, anticodon-binding domain | 647 - 827 | 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 |
| MVRKMSEQKD | YKNTLNLPET | GFPMRGDLAK | REPGMLKNWY | DNDLYQKIRQ | SSKGKKSFIL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HDGPPYANGS | IHIGHAVNKI | LKDIIIKSKT | ALGFDSPYIP | GWDCHGLPIE | LKVEGLVGKP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NQKISAAQFR | EECRKYAREQ | VEGQKKDFIR | LGVLGDWDNP | YLTMNFDTEA | NIIRAFGKAV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ANGHLYKGSK | PVHWCLDCAS | SLAEAEVEYE | DRTSPSIYVR | FAAADESAVE | NKFVLTEQGK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GKLSAVIWTT | TPWTLPSNKA | ISINPELEYQ | IVQFGDERFI | LAAELVESVA | QAVGVESWKA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LGSAKGSDLE | LLQFKHPFYD | YNVPFILGDH | VTLDGGTGLV | HTAPDHGQDD | YVVARKYNIG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MAGLIGNDGK | FNSNAKFFAG | LGVFEANGKV | LEKLDEVGAL | LKLEKIRHSY | PHCWRHKTPI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IFRATPQWFI | GMETQGLRQQ | ALSEIKKVRW | IPDWGQARIE | KMVENRPDWC | ISRQRTWGVP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VALFIHKETE | QLHPRTLELI | EEVAKLVERK | GIQAWWDLDA | KDLLGDDAAH | YSKVPDTLDV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| WFDSGSTYYS | VVKNRPEFNG | KEADMYLEGS | DQHRGWFMSS | LMLSTATDNK | APYKQVLTHG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FTVDGQGRKM | SKSIGNIVTP | QEVMDKFGGD | ILRLWVASTD | YTGEMTVSDE | ILKRAADSYR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RIRNTARFLL | ANLNGFDPKR | DLVQAHEMIS | LDRWAVDCAF | RAQAEIKEAY | DNYQFHTVVQ |
| 730 | 740 | 750 | 760 | 770 | 780 |
| RLMKFCSVEM | GSFYLDIIKD | RQYTTKADSL | ARRSCQTALW | HIAEALVRWM | APILSFTADE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| IWGYLPGERG | EFVFTEEFYD | GLFALDVSES | LDDAYWQQVI | TVRNEVNRVL | EQARNDKVIG |
| 850 | 860 | 870 | 880 | 890 | 900 |
| GGLEAEVTIF | ANDEYSALLN | KLGNELRFVT | ITSKAEVKTL | ADADVAEGEV | AGLAIKAIRS |
| 910 | 920 | 930 | |||
| ANHKCPRCWH | YSDSKDANSL | CSRCEENVNG | NGEERRFA |