A9M1Q6
Gene name |
serS |
Protein name |
Serine--tRNA ligase |
Names |
Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase |
Species |
Neisseria meningitidis serogroup C (strain 053442) |
KEGG Pathway |
nmn:NMCC_1597 |
EC number |
6.1.1.11: 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 A9M1Q6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9M1Q6-F1 | Predicted | AlphaFoldDB |
No variants for A9M1Q6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9M1Q6 | |||||
No associated diseases with A9M1Q6
4 regional properties for A9M1Q6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 226 - 405 | IPR002314 |
| domain | Aminoacyl-tRNA synthetase, class II | 172 - 415 | IPR006195 |
| domain | Serine-tRNA synthetase, type1, N-terminal | 1 - 109 | IPR015866 |
| domain | Serine-tRNA ligase catalytic core domain | 121 - 422 | IPR033729 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.11 | 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| serine-tRNA ligase activity | Catalysis of the reaction: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| selenocysteine biosynthetic process | The chemical reactions and pathways resulting in the formation of selenocysteine, an essential component of glutathione peroxidase and some other proteins. |
| selenocysteinyl-tRNA(Sec) biosynthetic process | The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA |
| seryl-tRNA aminoacylation | The process of coupling serine to seryl-tRNA, catalyzed by seryl-tRNA synthetase. The seryl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a serine-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 |
| MLDIQLLRSN | TAAVAERLAA | RGYEFDAARF | NALEEQRKAV | QVKTEELQAS | RNSISKQIGA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LKGQGKHEEA | QAAMDQVAQI | KTDLEQAAAD | LDAVQKELDA | WLLSIPNLPH | ESVPAGKDET |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ENVEVRKVGT | PREFDFEIKD | HVDLGEPLGL | DFEGGAKLSG | ARFTVMRGQI | ARLHRALAQF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MLDTHTLQHG | YTEHYTPYIV | DDTTLQGTGQ | LPKFAEDLFH | VTRGGDETKT | TQYLIPTAEV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TLTNTVADSI | IPSEQLPLKL | TAHSPCFRSE | AGSYGKDTRG | LIRQHQFDKV | EMVQIVHPEK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SYETLEEMVG | HAENILKALE | LPYRVITLCT | GDMGFGAAKT | YDLEVWVPAQ | NTYREISSCS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NCEDFQARRM | KARFKDENGK | NRLVHTLNGS | GLAVGRTLVA | VLENHQNADG | SINIPAALQP |
| 430 | |||||
| YMGGVAKLEV | K |