Annotations: 4AKF

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	flgH_like	e4akfA3	A: alpha bundles	X: ExoU toxin middle helical domain (From Topology)	H: ExoU toxin middle helical domain (From Topology)	T: ExoU toxin middle helical domain	F: flgH_like	ECOD (1.6)
A	Patatin	e4akfA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: Patatin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1090.10	Alpha Beta	3-Layer(aba) Sandwich	Cytosolic phospholipase A2 catalytic domain	Cytosolic phospholipase A2 catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01734	Patatin-like phospholipase (Patatin)	Patatin-like phospholipase	This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers [2]. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrol ...	This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers [2]. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids [2]. Members of this family have been found also in vertebrates.	Domain
A	PF22140	VipD-like, C-terminal domain (VipD-like_C)	VipD-like, C-terminal domain	This domain is found in VipD from Legionella pneumophila (effector vacuolar protein sorting inhibitor protein D), which localises to early endosomal membranes and alters their lipid and protein composition. This process protects the pathogen from end ...	This domain is found in VipD from Legionella pneumophila (effector vacuolar protein sorting inhibitor protein D), which localises to early endosomal membranes and alters their lipid and protein composition. This process protects the pathogen from endosomal fusion. VipD adopts a two-domain fold, with a N-terminal domain homologous to patatin (Pfam:PF01734) and a C-terminal domain (this entry) that contains ten alpha-helices and two short beta-strands. VipD localises to early endosomes via this domain [1,2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	VIPD	hydrolase activity catalytic activity	lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process symbiont-mediated perturbation of host cellular process biological process involved in interspecies interaction between organisms symbiont-mediated perturbation of host process symbiont-mediated perturbation of host vesicle-mediated transport modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
A	IPR054392	VipD-like, C-terminal domain	Domain
A	IPR002641	Patatin-like phospholipase domain	Domain
A	IPR052580	Probable Lipid Hydrolase	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.