P34945
Gene name |
serS (TT_C0520) |
Protein name |
Serine--tRNA ligase |
Names |
Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase |
Species |
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) |
KEGG Pathway |
tth:TT_C0520 |
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
10 structures for P34945
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1SER | X-ray | 290 A | A/B | 1-421 | PDB |
| 1SES | X-ray | 250 A | A/B | 1-421 | PDB |
| 1SET | X-ray | 255 A | A/B | 1-421 | PDB |
| 1SRY | X-ray | 250 A | A/B | 1-421 | PDB |
| 3ERR | X-ray | 227 A | A/B | 94-419 | PDB |
| 5EIU | X-ray | 191 A | A/D | 49-78 | PDB |
| 5F7T | X-ray | 229 A | E/F/H/L | 49-78 | PDB |
| 5IEA | X-ray | 326 A | A/B/C/D/F/K | 49-78 | PDB |
| 5VA4 | X-ray | 231 A | A | 49-78 | PDB |
| AF-P34945-F1 | Predicted | AlphaFoldDB |
No variants for P34945
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P34945 | |||||
No associated diseases with P34945
4 regional properties for P34945
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 218 - 395 | IPR002314 |
| domain | Aminoacyl-tRNA synthetase, class II | 135 - 405 | IPR006195 |
| domain | Serine-tRNA synthetase, type1, N-terminal | 1 - 102 | IPR015866 |
| domain | Serine-tRNA ligase catalytic core domain | 116 - 412 | 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. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| identical protein binding | Binding to an identical protein or proteins. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| serine binding | Binding to 2-amino-3-hydroxypropanoic acid. |
| serine-tRNA ligase activity | Catalysis of the reaction: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). |
| tRNA binding | Binding to a transfer RNA. |
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 |
| MVDLKRLRQE | PEVFHRAIRE | KGVALDLEAL | LALDREVQEL | KKRLQEVQTE | RNQVAKRVPK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| APPEEKEALI | ARGKALGEEA | KRLEEALREK | EARLEALLLQ | VPLPPWPGAP | VGGEEANREI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KRVGGPPEFS | FPPLDHVALM | EKNGWWEPRI | SQVSGSRSYA | LKGDLALYEL | ALLRFAMDFM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ARRGFLPMTL | PSYAREKAFL | GTGHFPAYRD | QVWAIAETDL | YLTGTAEVVL | NALHSGEILP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YEALPLRYAG | YAPAFRSEAG | SFGKDVRGLM | RVHQFHKVEQ | YVLTEASLEA | SDRAFQELLE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NAEEILRLLE | LPYRLVEVAT | GDMGPGKWRQ | VDIEVYLPSE | GRYRETHSCS | ALLDWQARRA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NLRYRDPEGR | VRYAYTLNNT | ALATPRILAM | LLENHQLQDG | RVRVPQALIP | YMGKEVLEPC |
| G |