P32048
Gene name |
MSK1 (YNL073W, N2364) |
Protein name |
Lysine--tRNA ligase, mitochondrial |
Names |
Lysyl-tRNA synthetase, LysRS |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YNL073W |
EC number |
6.1.1.6: 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 P32048
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P32048-F1 | Predicted | AlphaFoldDB |
16 variants for P32048
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s14-488588 | 68 | L>F | No | SGRP | |
| s14-488595 | 70 | Q>R | No | SGRP | |
| s14-488599 | 71 | E>D | No | SGRP | |
| s14-488654 | 90 | T>A | No | SGRP | |
| s14-488760 | 125 | G>A | No | SGRP | |
| s14-488797 | 137 | L>F | No | SGRP | |
| s14-488976 | 197 | S>L | No | SGRP | |
| s14-489386 | 334 | T>A | No | SGRP | |
| s14-489387 | 334 | T>I | No | SGRP | |
| s14-489398 | 338 | D>Y | No | SGRP | |
| s14-489588 | 401 | N>S | No | SGRP | |
| s14-489632 | 416 | K>E | No | SGRP | |
| s14-489648 | 421 | S>F | No | SGRP | |
| s14-489672 | 429 | S>F | No | SGRP | |
| s14-489827 | 481 | V>I | No | SGRP | |
| s14-489977 | 531 | V>I | No | SGRP |
No associated diseases with P32048
9 regional properties for P32048
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 214 - 568 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 102 - 192 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 229 - 566 | IPR006195 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 242 - 252 | IPR018149-1 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 258 - 274 | IPR018149-2 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 286 - 299 | IPR018149-3 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 304 - 321 | IPR018149-4 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 451 - 467 | IPR018149-5 |
| domain | Lysine-tRNA ligase, class II, N-terminal | 101 - 219 | IPR044136 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.6 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| lysine-tRNA ligase activity | Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). |
| tRNA binding | Binding to a transfer RNA. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| lysyl-tRNA aminoacylation | The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA. |
| mitochondrial lysyl-tRNA aminoacylation | The process of coupling lysine to lysyl-tRNA in a mitochondrion, catalyzed by lysyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. |
| mitochondrial translation | The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code. |
| tRNA processing | The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P15180 | KRS1 | Lysine--tRNA ligase, cytoplasmic | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P0A8N5 | lysU | Lysine--tRNA ligase, heat inducible | Escherichia coli (strain K12) | PR |
| P0A8N3 | lysS | Lysine--tRNA ligase | Escherichia coli (strain K12) | PR |
| Q6F2U9 | Os03g0586800 | Lysine--tRNA ligase | Oryza sativa subsp japonica (Rice) | PR |
| Q22099 | kars-1 | Lysine--tRNA ligase | Caenorhabditis elegans | PR |
| Q9ZPI1 | At3g11710 | Lysine--tRNA ligase, cytoplasmic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q43776 | LYSRS | Lysine--tRNA ligase | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNVLLKRRSL | TFAPRWLWCK | CRSSRSRPYS | LAHAVDTSKM | EATRRNGQIV | KDLGRYYPSM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SESALHDLCQ | EYKEVTIADF | NERFLGNPAT | LHHEDNPNLL | LSINGRIKSI | RFSGQKIVFI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DLYNGSSGLK | NDTQLQLIVN | YNKIGGSSED | KANFSEYMNF | LKKGDYIKAL | GYPGFSQSRV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KMLSLICNKL | PIVLSVSQLP | LPSRLNDETK | IKSNRVVDYQ | LNGTQTLLVR | ARIIKLLRKF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LDDRNFVEVE | TPILSSKSNG | AMAKPFITSS | KDFDHLELRI | APELWLKRLI | ISGLQKVYEI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GKVFRNEGID | STHNAEFSTL | EFYETYMSMD | DIVTRTEDLF | KFLITNLQKF | FQDTRLPVPK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TFSELHLALS | ENNWKFRKVE | FLPTLNKELG | IDLMNSGLDI | NKPSELLKAL | PKDIAKKYFP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SADNTGQLSS | LQILNKLSDV | FLEQRHCQST | LPTVIYHQPA | ILSPLAKTDP | QNKQVTKRFE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VFIKGKEYIN | AYEEENCPQL | QLQKFLQQKQ | INELTGNKTE | TLSPVIDYQY | VETMKYGMPP |
| 550 | 560 | 570 | |||
| VGGFGLGIDR | LCMLFCDKKR | IEEVLPFGCV | DDVNRQ |