B0JN99
Gene name |
asnS |
Protein name |
Asparagine--tRNA ligase |
Names |
Asparaginyl-tRNA synthetase, AsnRS |
Species |
Microcystis aeruginosa (strain NIES-843 / IAM M-2473) |
KEGG Pathway |
mar:MAE_04410 |
EC number |
6.1.1.22: 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 B0JN99
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B0JN99-F1 | Predicted | AlphaFoldDB |
No variants for B0JN99
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B0JN99 | |||||
No associated diseases with B0JN99
3 regional properties for B0JN99
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Chorismate synthase, conserved site | 16 - 31 | IPR020541-1 |
| conserved_site | Chorismate synthase, conserved site | 124 - 140 | IPR020541-2 |
| conserved_site | Chorismate synthase, conserved site | 327 - 343 | IPR020541-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.22 | 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 |
|---|---|
| asparagine-tRNA ligase activity | Catalysis of the reaction: L-asparagine + ATP + tRNA(Asn) = AMP + Asn-tRNA(Asn) + diphosphate + 2 H(+). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| nucleic acid binding | Binding to a nucleic acid. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| asparaginyl-tRNA aminoacylation | The process of coupling asparagine to asparaginyl-tRNA, catalyzed by asparaginyl-tRNA synthetase. The asparaginyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an asparagine-accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTRIKEIFQ | TGQPDQSVTV | QGWVRTKREL | KEFTFLEVND | GSSLANLQVI | LEPTLPDYEN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VLKTISTGAA | IAVSGNLVPS | PGKGQNIELK | AAEITLYGDC | PPDYPLQKKR | HSFEFLRTIA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HLRARTNTLG | AVMRVRNACA | TAIHSFFQEK | GFIWVHTPII | TANDCEGAGE | LFTVTSLDLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KPANFAEDFF | GKRAYLTVSG | QLQAEVMAMA | LSNVYTFGPT | FRAENSNTSR | HLAEFWMVEP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EMAFCDLEGD | QDLAEAFLKY | IFKFVLENCP | EDLQFFNERI | DKTVLSTAEN | IVNSEFGRIT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YSEAIELLEK | ADRQFEFPVE | WGVDLQSEHE | RYLAEELFKK | PVIVTNYPKT | IKAFYMRLDD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NNKTVSAMDI | LAPKIGEIIG | GSQREERLDV | LIQRMQEQGM | NPDDLWWYLD | LRRYGSVPHA |
| 430 | 440 | 450 | |||
| GFGLGFERLV | QFMTGMTNIR | DVIPFPRTPL | SADF |