Q58659
Gene name |
metG |
Protein name |
Methionine--tRNA ligase |
Names |
Methionyl-tRNA synthetase, MetRS |
Species |
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
KEGG Pathway |
mja:MJ_1263 |
EC number |
6.1.1.10: 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 Q58659
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58659-F1 | Predicted | AlphaFoldDB |
No variants for Q58659
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58659 | |||||
No associated diseases with Q58659
6 regional properties for Q58659
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA-binding domain | 550 - 651 | IPR002547 |
| domain | Methionyl-tRNA synthetase, beta subunit, C-terminal | 519 - 651 | IPR004495 |
| domain | Methionyl/Leucyl tRNA synthetase | 3 - 384 | IPR015413 |
| domain | Methioninyl-tRNA synthetase core domain | 2 - 359 | IPR033911-1 |
| domain | Methioninyl-tRNA synthetase core domain | 371 - 382 | IPR033911-2 |
| domain | Methionyl-tRNA synthetase, anticodon-binding domain | 368 - 529 | IPR041872 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.10 | 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 |
|---|---|
| aminoacyl-tRNA synthetase multienzyme complex | A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| methionine-tRNA ligase activity | Catalysis of the reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| methionyl-tRNA aminoacylation | The process of coupling methionine to methionyl-tRNA, catalyzed by methionyl-tRNA synthetase. The methionyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a methionine-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 |
| MRYLITTALA | YTNGPLHLGH | ARSTYIPADI | IYKYLKLRGE | DVIHVGGTDN | HGVPITLTAE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KEGKSPEEIV | EKYHNEIKED | LDLLGVEFDA | FGKTHSQIHI | ETAQEFYLKL | KENGYIYEKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IEQFYCPNCK | KFLPDRYVEG | ICPYCGGEAR | GDHCEVCGRH | LEPFELKDPY | CVICKGKPEI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RKTKHHFFKL | SALKKELEEY | IKNAKEMPEH | VKNMALNWIK | ELHDWDISRD | ISWGVPIPGT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NQVMYVWLEA | PIGYISFTKM | LGEIWKKYWL | EKDTKIYHFI | GKDITVHHAV | FWPGMLIAHG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SFNLPTAVVS | GGYLTLEGRK | MSTSKRWVVW | VKDFVKNFDA | DYLRYYLIMS | APLFKDCDFS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FDDFKNKINN | ELINIIGNFT | HRVLTFTHRK | FKKVPIVDED | RLKEEDKELL | KKCEETLEAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DKNIRSFKFR | DALVNILHLA | IEGNSYFQKM | EPWAVDDEER | LKEILYTCCK | TVKTLVYLLY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PYMPKKSLAL | LELMNEELDL | ELRGNELKKP | KIIFKKIDNK | KIEEMKKKLY | ENKKEETKGG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EKMEQIDISY | LEKIDLRVGE | VVEAEDIPKS | KKLLKLMVDL | GDEKRQIVSG | IKGYYKPEDL |
| 610 | 620 | 630 | 640 | 650 | |
| VGKKVIVICN | LKPAKLCGVL | SEGMILAAED | DEGNVSLLTV | DKDIKAGSKV | R |