A9BDK6
Gene name |
ileS |
Protein name |
Isoleucine--tRNA ligase |
Names |
Isoleucyl-tRNA synthetase, IleRS |
Species |
Prochlorococcus marinus (strain MIT 9211) |
KEGG Pathway |
pmj:P9211_02611 |
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 A9BDK6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9BDK6-F1 | Predicted | AlphaFoldDB |
No variants for A9BDK6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9BDK6 | |||||
No associated diseases with A9BDK6
5 regional properties for A9BDK6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 68 - 79 | IPR001412 |
| domain | Aminoacyl-tRNA synthetase, class Ia | 40 - 671 | IPR002300 |
| domain | Zinc finger, FPG/IleRS-type | 938 - 964 | IPR010663 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 718 - 867 | IPR013155 |
| domain | Isoleucyl tRNA synthetase type 1, anticodon-binding domain | 673 - 852 | 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 |
| MTKETRQGEQ | NRPSYKESLN | LLKTSFGMRA | NATLREPELQ | NFWADKGIDL | ELGLANKGPS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FTLHDGPPYA | NGALHMGHAL | NKVLKDIINK | FHIMRGHKVH | FVPGWDCHGL | PIELKVLQTL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SNKERQALTP | IQLRKKAAAY | ASKQVKGQME | GFKRWGIWGN | WNKPYLTLQK | EYESAQVKLF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GQMVLKGYIY | RGLKPVHWSP | SSRTALAEAE | LEYPEAHTSP | SVYVAFSVIH | LPQSLSENLI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KQGLELPGDE | VELSKRLKVC | IWTTTPWTLP | ANAAVSVNSN | LDYSFVRHEE | KGQILIFATE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLEEVSEILG | ISFKQVANAK | GESLKGILYK | HPLYERTAPI | VLGGSYITTQ | SGTGLVHTAP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GHGIDDFKTG | LQNNLEVFCP | VDEKGIFTSE | AGKFEGLNVL | KDANKEIISS | LEISGSLLKE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LPYVHKYPYD | WRTKKPTIFR | ATEQWFASVE | GFREDALKAI | DDVEWLPESG | RNRIQSMVRE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RGDWCISRQR | TWGIPIPVFY | KKNTNEILLN | KETIDHIENL | FAQYGADIWW | EFDESKLLPP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SLASESHHWQ | KGVDTMDVWF | DSGSSWASVS | CQRDELGYPA | DLYLEGTDQH | RGWFQSSLLT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SVAVNGHAPY | KKVLTHGFAL | DENGRKMSKS | LGNIIDPTVI | INGGTNKKTD | PAYGADVLRL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| WVSSVDYSVD | VPIGSNILKQ | LSDVYRKVRN | TSRYLLGNLH | DFDPKKNSVD | IDNLPILDKW |
| 730 | 740 | 750 | 760 | 770 | 780 |
| MLNRTAEVID | EITLAFEKYE | FSRFFQLLQS | FCTVDLSNFY | LDIAKDRLYV | SAPDDPRRRA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| CQTVMALIIE | KLAGLISPVL | CHMAEDIWQN | IPYQLSEESV | FKRGWPVSPS | NWKRASLTEP |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ISLIRELRTS | VNRVLEGCRN | RQELGSSLEA | GLRLEITNQG | LLDAIDFLAK | NGDHDVDCIR |
| 910 | 920 | 930 | 940 | 950 | 960 |
| DWFLVSQLQI | GGEPWAEVLI | SQQFELGVIE | ISNARGYKCE | RCWHYEQDIG | SCSEHPTLCG |
| RCVTVMNRL |