Q5XH07
Gene name |
thnsl2 |
Protein name |
Threonine synthase-like 2 |
Names |
TSH2 |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:495098 |
EC number |
|
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 Q5XH07
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5XH07-F1 | Predicted | AlphaFoldDB |
No variants for Q5XH07
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5XH07 | |||||
No associated diseases with Q5XH07
No regional properties for Q5XH07
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5XH07 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| lyase activity | Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKYTSTRGGL | IGVDFEGVLF | SGFAPDGGLF | MPEDIPKVDK | RTLQTWSSYS | YIQLVKEICS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFISPESIPR | ADLEGLIDRA | FIRFRHRDIV | PITRLKSGLN | VMEMWHGVTH | AFKDLAMSCV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GELLDYFLKR | KNKHVTILVA | TSGDTGSSAI | ESVRRRENMD | IIVLLPHGRC | TKIQELQMTT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VIEDNVHVFS | VDGTSDELDY | PIKRLFADSD | FVKKHNIMST | NSVNWARILV | QIAHFFYGYM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QCAPLTELTP | VEIIVPTGGA | GNITAGCIAQ | AMGLPIHLVA | VVNRNDIVHR | TVQYGDFSLG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DTKATLASAM | DIQEPYNMER | ILWLLAGSEK | SHIKEMMKEF | QEKKRVKLPE | QLHKKIAGAM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TSCVVTDENI | LGTIGRCWEE | NHYLLCPHSA | VAVYYHYQQM | DSNDKSPRCC | LAPASAAKFQ |
| 430 | 440 | 450 | 460 | 470 | |
| DVIIKANLTP | DIPQEIKDLE | KKKTRSHHLT | KEDDWEKVLR | QTIESISQRK | VQ |