Q5BMR2 (PLD_PHYIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 25.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Phospholipase D EC=3.1.4.4 Alternative name(s): PiPLD1 | ||
| Gene names |
| ||
| Organism | Phytophthora infestans (Potato late blight fungus) | ||
| Taxonomic identifier | 4787 [NCBI] | ||
| Taxonomic lineage | Eukaryota › stramenopiles › Oomycetes › Peronosporales › Phytophthora |
Protein attributes
| Sequence length | 1807 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. |
| Catalytic activity | A phosphatidylcholine + H2O = choline + a phosphatidate. |
| Subcellular location | Membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the phospholipase D family. TM-PLD subfamily. Contains 2 PLD phosphodiesterase domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Membrane |
| Domain | Repeat Transmembrane Transmembrane helix |
| Molecular function | Hydrolase |
| Gene Ontology (GO) | |
| Biological process | glycerophospholipid catabolic process Non-traceable author statement Ref.1. Source: UniProtKB |
| Cellular component | integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB |
| Molecular function | NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phospholipase D activityNon-traceable author statement Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1807 | 1807 | Phospholipase D | PRO_0000239465 | |||||
Regions | |||||||||
| Transmembrane | 257 – 277 | 21 | Helical; Potential | ||||||
| Transmembrane | 305 – 325 | 21 | Helical; Potential | ||||||
| Transmembrane | 587 – 607 | 21 | Helical; Potential | ||||||
| Domain | 853 – 880 | 28 | PLD phosphodiesterase 1 | ||||||
| Domain | 1249 – 1276 | 28 | PLD phosphodiesterase 2 | ||||||
Sites | |||||||||
| Active site | 858 | 1 | Potential | ||||||
| Active site | 860 | 1 | Potential | ||||||
| Active site | 865 | 1 | Potential | ||||||
| Active site | 1254 | 1 | Potential | ||||||
| Active site | 1256 | 1 | Potential | ||||||
| Active site | 1261 | 1 | Potential | ||||||
Sequences
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References
| [1] | "A transmembrane phospholipase D in Phytophthora; a novel PLD subfamily." Meijer H.J.G., Latijnhouwers M., Ligterink W., Govers F. Gene 350:173-182(2005) [PubMed: 15826868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY929154 Genomic DNA. Translation: AAX28839.1. |
3D structure databases | |
| ProteinModelPortal | Q5BMR2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR015679. PLipase_D. IPR001736. PLipase_D/transphosphatidylase. [Graphical view] |
| PANTHER | PTHR18896. Phospholipase_D. 1 hit. |
| Pfam | PF00614. PLDc. 1 hit. [Graphical view] |
| SMART | SM00155. PLDc. 2 hits. [Graphical view] |
| PROSITE | PS50035. PLD. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLD_PHYIN | ||||||||
| Accession | Primary (citable) accession number: Q5BMR2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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