A8MA54
Gene name |
metG |
Protein name |
Methionine--tRNA ligase |
Names |
Methionyl-tRNA synthetase, MetRS |
Species |
Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167) |
KEGG Pathway |
cma:Cmaq_0136 |
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 A8MA54
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A8MA54-F1 | Predicted | AlphaFoldDB |
No variants for A8MA54
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A8MA54 | |||||
No associated diseases with A8MA54
4 regional properties for A8MA54
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Methionyl/Leucyl tRNA synthetase | 18 - 410 | IPR015413 |
| domain | Methioninyl-tRNA synthetase core domain | 18 - 385 | IPR033911-1 |
| domain | Methioninyl-tRNA synthetase core domain | 397 - 408 | IPR033911-2 |
| domain | Methionyl-tRNA synthetase, anticodon-binding domain | 394 - 558 | 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 |
| MLDRRIFSDP | NGNEVRWVVG | SAWPYIYAVP | HLGNLIGSLL | SADVFTRYLK | LKGYDVVFVT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GSDEHGTPIE | VEAIKLGIEP | RQLTDRMHEI | IVKLLKLWGI | EPDNYTRTES | EVHKWYVRDA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FTKIYNNGYI | FTKDDELPYC | PRDKIFLPDR | FVIGTCPYCG | YPYARGDQCE | NCGRLLEPRM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LINPKCAICG | STPEWRLTRH | WYLDLRRLED | RIRSYIEGNS | ALPDNAKQMS | LGILKEGLRP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RAITRDNKWG | IPAPFPGAEG | KTIYVWFEAV | LGYVSATIEY | FRRLGREDDW | RRFWFNKGTR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VVFFIGKDNI | PFHTIIFPAL | LMATGEDYVM | PWTTSSTEYL | IFEGKKFSKS | QRVGIWADEA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IALLPADYWR | FYLIYNRPEQ | RDSNFTWDSF | LDVVNSIMND | TVGNFIHRVL | TLAKRRWGTV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PGDVKMIEQD | QEIYGKVLEI | LNTVEEDYER | IMLKDAVSQS | IEIARIGNKY | LNERQPWRLS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EVEFNSAIYM | LMSIVKTLSI | TLAPVIPFSI | NELWRMMGYS | NGLRWGDARK | PIEQGLRLSE |
| 550 | 560 | 570 | 580 | ||
| PKPLFRKISK | EELNVMLKKL | DEIRDIKDKG | KYPWEQAYLP | NP |