B3MTI8
Gene name |
fig |
Protein name |
Protein phosphatase PTC7 homolog fig |
Names |
Fos intronic gene protein |
Species |
Drosophila ananassae (Fruit fly) |
KEGG Pathway |
dan:6505517 |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
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 B3MTI8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B3MTI8-F1 | Predicted | AlphaFoldDB |
No variants for B3MTI8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B3MTI8 | |||||
No associated diseases with B3MTI8
1 regional properties for B3MTI8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PPM-type phosphatase-like domain | 65 - 325 | IPR001932 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| myosin phosphatase activity | Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. |
| protein serine/threonine phosphatase activity | Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| dephosphorylation | The process of removing one or more phosphoric (ester or anhydride) residues from a molecule. |
| regulation of ubiquinone biosynthetic process | Any process that modulates the frequency, rate or extent of ubiquinone biosynthesis. Ubiquinone biosynthesis consists of the chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKPTMMSNWP | GFINRFVRQV | RHPLDFRRPY | RITGFPDNLS | PLGYFGQTKQ | YARAAQEPYL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VTVVQGRSKK | PCSPRERANR | RFGEDSWFVS | STPRAEVLGV | ADGVGGWRDM | GVDAGRFAKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LMGCCCGRSE | QEDFDGRNPR | SLLVSSYQEL | KDRDDPVVGS | STACVVAMHR | RDLTLYTANL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GDSGFMVLRN | GRVMHRSEEQ | THDFNTPFQL | TVAPSHKLDS | VHCDGPEKAA | VSRHPLAPGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LVLLATDGLF | DNLPESMLLE | MLRKFHGVRD | EKELQDAANQ | VVEKARELSM | NASFPSPFAV |
| 310 | 320 | 330 | |||
| KARANNISYS | GGGKPDDITL | ILASVEVPKV | HR |