A3PLG8
Gene name |
metG |
Protein name |
Methionine--tRNA ligase |
Names |
Methionyl-tRNA synthetase, MetRS |
Species |
Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter sphaeroides) |
KEGG Pathway |
rsh:Rsph17029_2081 |
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 A3PLG8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A3PLG8-F1 | Predicted | AlphaFoldDB |
No variants for A3PLG8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A3PLG8 | |||||
No associated diseases with A3PLG8
4 regional properties for A3PLG8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Methionyl/Leucyl tRNA synthetase | 4 - 409 | IPR015413 |
| domain | Methioninyl-tRNA synthetase core domain | 3 - 385 | IPR033911-1 |
| domain | Methioninyl-tRNA synthetase core domain | 397 - 408 | IPR033911-2 |
| domain | Methionyl-tRNA synthetase, anticodon-binding domain | 394 - 571 | 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 | |
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. |
3 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). |
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 |
| MARILITSAI | PYINGIKHLG | NLVGSQLPAD | LYARYMRGRG | HEVMFICATD | EHGTPAELAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AKAGKPVEDY | CAEMHEVQKE | IAAGFRLSFD | HFGRSSSARN | HRLTQHFAGA | LAENGFIEEV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VERQFFSVAD | NRFLPDRYIE | GTCPNCGYDK | ARGDQCENCT | KQLDPTDLID | PRSAISGSTE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LELRETKHLY | LRQRALKDEI | EAWIDSKTDW | PVLTTSIAKK | WLHDGEGLQD | RGITRDLKWG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VPVRKGSEPW | PGMEGKVFYV | WFDAPIEYIA | GTAEWADANG | KTDADWERWW | RTDRGAEDVR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YVQFMGKDNV | PFHTLSFPAT | IMGSREPWKL | VDYIKSFNYL | NYDGGQFSTS | QGRGVFMDQA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSILPADYWR | WWLLSHAPEN | SDSEFTWENF | QSSVNKDLAD | VLGNLVSRVT | KFCRSKFGET |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VPAGGSPGER | EHQLVAELQQ | RLAAYEACME | AMEVRKAASE | LRALWVAGNE | YLQSAAPWTV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VKTDPEQAQA | MIRLALNLIR | LYAVISRPFI | PDAAASMMTS | LGCEDWSWPA | DVGRALEVLP |
| 550 | 560 | 570 | |||
| AGHGFTTPEV | LFRKITDEER | AEWQTRFSGV | RS |