Q9JJL8
Gene name |
Sars2 (Sarsm) |
Protein name |
Serine--tRNA ligase, mitochondrial |
Names |
SerRSmt, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:71984 |
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 Q9JJL8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JJL8-F1 | Predicted | AlphaFoldDB |
26 variants for Q9JJL8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388885653 | 12 | F>V | No | EVA | |
| rs223730991 | 25 | V>M | No | EVA | |
| rs3388882545 | 27 | S>I | No | EVA | |
| rs3388896802 | 32 | R>W | No | EVA | |
| rs246256556 | 60 | M>L | No | EVA | |
| rs3388893002 | 73 | S>Y | No | EVA | |
| rs212438917 | 116 | A>S | No | EVA | |
| rs3388898047 | 130 | Q>* | No | EVA | |
| rs3388890312 | 138 | L>M | No | EVA | |
| rs3388898834 | 148 | Q>* | No | EVA | |
| rs3388885707 | 182 | D>N | No | EVA | |
| rs3388854120 | 188 | V>M | No | EVA | |
| rs3388895194 | 191 | V>L | No | EVA | |
| rs3388873857 | 211 | K>I | No | EVA | |
| rs47185959 | 253 | R>K | No | EVA | |
| rs3397634389 | 262 | D>V | No | EVA | |
| rs3397305352 | 264 | L>Q | No | EVA | |
| rs3397724550 | 265 | R>G | No | EVA | |
| rs3388890452 | 267 | A>V | No | EVA | |
| rs244040233 | 274 | M>I | No | EVA | |
| rs3388892933 | 314 | A>G | No | EVA | |
| rs3388896706 | 336 | G>V | No | EVA | |
| rs3388898848 | 360 | G>E | No | EVA | |
| rs3388892983 | 362 | E>G | No | EVA | |
| rs3388885633 | 385 | H>Y | No | EVA | |
| rs3388876647 | 508 | K>M | No | EVA |
No associated diseases with Q9JJL8
4 regional properties for Q9JJL8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 291 - 468 | IPR002314 |
| domain | Aminoacyl-tRNA synthetase, class II | 202 - 478 | IPR006195 |
| domain | Serine-tRNA synthetase, type1, N-terminal | 59 - 172 | IPR015866 |
| domain | Serine-tRNA ligase catalytic core domain | 185 - 485 | 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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
3 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). |
| tRNA binding | Binding to a transfer RNA. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| mitochondrial seryl-tRNA aminoacylation | The process of coupling serine to seryl-tRNA in a mitochondrion, catalyzed by seryl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. |
| 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. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAASMARLWW | PFLARQGLRS | RGRCVCSQNP | RRSFATEKRV | RNLLYEHARE | GYSELPYLDM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ESVCACPEKA | ARSLELRKGE | LRPADLPAII | STWQELRQLR | EQIRSLEAEK | EAVAEAVRAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LANQDSDQVQ | KDPQYQGLRA | RGREIRKQLT | PLYPQETQLE | EQLYQQALRL | PNQTHPDTPV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GDESQARVVR | VVGEKPAFSF | QPRGHLEIGE | KLDIIRQKRL | SHVSGHRSYY | LRGAGALLQH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GLVNFTLSKL | VSRGFTPMTV | PDLLRGAVFE | GCGMTPNANP | SQIYNIDPSR | FEDLNLAGTA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EVGLAGYFMD | HSVAFRDLPV | RMVCASTCYR | AETDTGKEPW | GLYRVHHFTK | VEMFGVTGPG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LEQSSQLLDE | FLSLQVEILT | ELGLHFRVLD | MPTQELGLPA | YRKFDIEAWM | PGRGRYGEVT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SASNCTDFQS | RRLYIMFETE | TGELQFAHTV | NATACAVPRV | LIALLESNQQ | KDGSVLVPAA |
| 490 | 500 | 510 | |||
| LQPYLGTDRI | TAPTHVPLQY | IGPNQPQKPR | LPGQSATR |