A1TTU1
Gene name |
metG |
Protein name |
Methionine--tRNA ligase |
Names |
Methionyl-tRNA synthetase, MetRS |
Species |
Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp citrulli) |
KEGG Pathway |
aav:Aave_3834 |
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 A1TTU1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1TTU1-F1 | Predicted | AlphaFoldDB |
No variants for A1TTU1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1TTU1 | |||||
No associated diseases with A1TTU1
7 regional properties for A1TTU1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 13 - 24 | IPR001412 |
| domain | tRNA-binding domain | 600 - 706 | IPR002547 |
| domain | Methionyl-tRNA synthetase, beta subunit, C-terminal | 574 - 706 | IPR004495 |
| domain | Methionyl/Leucyl tRNA synthetase | 6 - 406 | IPR015413 |
| domain | Methioninyl-tRNA synthetase core domain | 5 - 382 | IPR033911-1 |
| domain | Methioninyl-tRNA synthetase core domain | 394 - 405 | IPR033911-2 |
| domain | Methionyl-tRNA synthetase, anticodon-binding domain | 385 - 553 | 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 |
| MPARKIFVTT | ALPYANGNFH | IGHIMEYIQA | DIWVRFQRMQ | GAEVNFVGAD | DTHGAPIMIA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEKAGKTPQQ | FVADIAAGRK | PYLEGFHIRF | DNWHSTDAPE | NHELARQIYR | DLQAAGLIET |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTIEQFFDPE | KNMFLPDRFI | KGECPRCHAR | DQYGDNCENC | GAVYAPTDLI | EPYSALSGAK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PVLKSSDHFF | FQLSDPRCVA | FLQEWTQDGR | LQPEVANKVK | EWFSVRTNPD | GTTSEGLGDW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DISRDAPYFG | IEIPDAPGKY | FYVWLDAPVG | YLASLKNLLE | KRGQSYDDYV | ADPQLEQVHF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGKDIVTFHT | LFWPAMLKFS | GRKTPDAVFV | HGFLTVNNGE | KMSKSRGTGL | DPLKYLGLGM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NAEWLRYYLA | AKLNGRNEDI | DFNAEDFMAR | VNSDLIGKFV | NIASRAAGFL | TKRFGGRLGA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PDADGAALLE | ALRAQAGAIA | EAYERRDTAR | AVRETMLLAD | RVNEYVDARK | PWELAKQEGQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EAALQAACTT | CIEAFRLLTL | YLKPVLPALA | AQVEAFLNVQ | PLTFADAPAL | LGEGHAIGAY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QHLMQRVDIK | QLEALFEVPA | AAAAPAAPAA | NAAAEASAAA | GAATEAPGGE | HIAPTITIDD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FAKIDLRIAL | IVNCEPVEGS | TKLLRLTLDV | GEGRHRNVFS | GIASAYRPEE | LVGKLTVMVA |
| 670 | 680 | 690 | 700 | ||
| NLAPRKMKFG | VSEGMVLAAS | HGDEKAHPGI | HVLNPWPGAT | PGMRVR |