A8H3V2
Gene name |
metG |
Protein name |
Methionine--tRNA ligase |
Names |
Methionyl-tRNA synthetase, MetRS |
Species |
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1) |
KEGG Pathway |
spl:Spea_1917 |
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 A8H3V2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A8H3V2-F1 | Predicted | AlphaFoldDB |
No variants for A8H3V2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A8H3V2 | |||||
No associated diseases with A8H3V2
7 regional properties for A8H3V2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 15 - 26 | IPR001412 |
| domain | tRNA-binding domain | 572 - 673 | IPR002547 |
| domain | Methionyl-tRNA synthetase, beta subunit, C-terminal | 538 - 673 | IPR004495 |
| domain | Methionyl/Leucyl tRNA synthetase | 8 - 396 | IPR015413 |
| domain | Methioninyl-tRNA synthetase core domain | 7 - 371 | IPR033911-1 |
| domain | Methioninyl-tRNA synthetase core domain | 384 - 395 | IPR033911-2 |
| domain | Methionyl-tRNA synthetase, anticodon-binding domain | 381 - 513 | 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. |
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 |
| MANSQRKILV | TSALPYANGP | IHLGHMLEYI | QTDIWSRFQK | LRGHECHYIC | ADDAHGTPIM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LKAQQLGMTP | EDMIAQVQKE | HEKDFADFNI | QFDNFHSTHS | DENRELASEI | YIKLRDAGYI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KTKTISQLFD | PEKSMFLPDR | FVKGTCPRCK | SEDQYGDNCD | NCGATYSTTD | LIDPKSAVSG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ATPVMKDTEH | FFFDLPSFEG | MLKEWINSGS | LQQEMANKLG | EWFEQGLQQW | DISRDAPYFG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FEIPDAPGKF | FYVWLDAPIG | YMGSFKNLCN | KRDDLNFDDF | WSKDSTAEVY | HFIGKDIVYF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HSLFWPAMLE | GAGLRKPTSV | YAHGYVTVNG | AKMSKSKGTF | IKARTYLDNL | DPEYLRYYYA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AKLSSRIDDL | DLNLEDFAQR | VNSDLVGKLV | NLASRTAGFI | SKRFDGKLAK | IADTSLTESF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LAKQETIANF | YETREFGKAM | REVMTLADIA | NAYVADSAPW | QLIKDDAKQE | EAHQVCTNAL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NLFRILVTYL | KPVLPKLAQD | VEAFLQMELT | WDNLDVDLAG | HEIAKFKALM | QRVEMKSIEA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IIEASKENLQ | VTAEPEVKKQ | DKTPLEQDPI | SEEISFEDFA | KIDLRIARIA | KAEHVKEANK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LLRLELDLGG | ETKQVFAGIK | SAYAPEDLEG | KLTVMVANLA | PRQMRFGVSE | GMVLAAGPGG |
| 670 | |||||
| KDLWIMEPHE | GAQPGMKVK |