P20419
Gene name |
plc (cbp) |
Protein name |
Phospholipase C |
Names |
PLC, Cbp, Phosphatidylcholine cholinephosphohydrolase |
Species |
Paraclostridium bifermentans (Clostridium bifermentans) |
KEGG Pathway |
|
EC number |
3.1.4.3: Phosphoric diester 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 P20419
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P20419-F1 | Predicted | AlphaFoldDB |
No variants for P20419
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P20419 | |||||
No associated diseases with P20419
4 regional properties for P20419
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phox homology | 208 - 379 | IPR001683 |
| domain | Phospholipase D/Transphosphatidylase | 641 - 668 | IPR001736-1 |
| domain | Phospholipase D/Transphosphatidylase | 941 - 968 | IPR001736-2 |
| domain | Phospholipase D-like domain | 815 - 984 | IPR025202 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.4.3 | Phosphoric diester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| phosphatidylcholine phospholipase C activity | Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H+ + phosphocholine. |
| toxin activity | Interacting selectively with one or more biological molecules in another (target) organism, initiating pathogenesis (leading to an abnormal, generally detrimental state) in the target organism. The activity should refer to an evolved function of the active gene product, i.e. one that was selected for. Examples include the activity of botulinum toxin, and snake venom. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| hemolysis in another organism | The cytolytic destruction of red blood cells, with the release of intracellular hemoglobin, in one organism by another. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKALKKVSNI | LCVLGLCTLM | GGTSYAWDGK | KDGTGTHSLI | AEHGLSMLNN | DLSGNESQQV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KDNIKILNEY | LGDLKLGSTY | PDYDPNAYDL | YQDHFYDPDT | GNNFTIDNSW | YASYPIYDTS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RNSVRKFATL | AKNEWEKGNF | KEATFLLGQG | LHYLGDLNTP | YHASNVTAVD | SPGHVKYETF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VEERKDNYAL | NTSGNDTTSG | VYKEAMENPS | FNKWMTQNSI | KYAKIAKDLY | YSHSTMSHSW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DDWDYSGREA | IKNSQVCTAG | FLYRFMNEVS | NGNTGDNDSL | TNEFNIVLKT | ADNKYAGTDD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NVYFGFETNE | GKKFEWKLDN | AGNDFERNQV | DNYILKTKDG | EEVDINNISN | YWIRKERLTS |
| 370 | 380 | 390 | |||
| ISDDWELSNF | KLIANGKVIQ | QQDVNKVFTG | NETYYINK |