A5DEQ9
Gene name |
SFH5 (PGUG_01760) |
Protein name |
Phosphatidylinositol transfer protein SFH5 |
Names |
PITP SFH5 |
Species |
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) |
KEGG Pathway |
pgu:PGUG_01760 |
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 A5DEQ9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5DEQ9-F1 | Predicted | AlphaFoldDB |
No variants for A5DEQ9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5DEQ9 | |||||
No associated diseases with A5DEQ9
1 regional properties for A5DEQ9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | CRAL-TRIO lipid binding domain | 131 - 308 | IPR001251 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| phosphatidylinositol transfer activity | Removes phosphatidylinositol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
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 |
| MSEPIEKPVE | KPGVEPVSDV | KDTDPAKKDQ | PVLVSTTKLT | KTQSETLKKL | IDELPQILEE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TGDSSYDEIY | GYRINKSGLE | HVHDEIRNEI | VLKFLIAEEY | KFEEARTRLI | NTFKWRKKFQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLSAAYSETF | DKELDDLGVI | TKYDGTNENL | HVVTWNLYGN | LKSPKKLFQK | FGQDDKAEKE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GSPFLRWRIG | LMERALSLID | FTDKSNSKIA | QVHDYNNVSM | FRMDPGMKAA | TKEIIKIFGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NYPELLSTKF | FINVPTIMSW | VFTFFRTIGL | VSEDTWKKFQ | VLNSGNLATW | FGEKNLPKAY |
| 310 | 320 | 330 | |||
| NGSNDSTVES | LFASEAKTEA | PEYAKIMIHK | AALDID |