Annotations: 1PRE

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1prea1	Alpha and beta proteins (a+b)	C-type lectin-like	C-type lectin-like	Aerolysin/Pertussis toxin (APT) domain	Proaerolysin, N-terminal domain	(Aeromonas hydrophila ) [TaxId: 644 ],	SCOPe (2.08)
A	d1prea2	Membrane and cell surface proteins and peptides	Aerolisin/ETX pore-forming domain	Aerolisin/ETX pore-forming domain	(Pro)aerolysin, pore-forming lobe	(Pro)aerolysin, pore-forming lobe	(Aeromonas hydrophila ) [TaxId: 644 ],	SCOPe (2.08)
B	d1preb1	Alpha and beta proteins (a+b)	C-type lectin-like	C-type lectin-like	Aerolysin/Pertussis toxin (APT) domain	Proaerolysin, N-terminal domain	(Aeromonas hydrophila ) [TaxId: 644 ],	SCOPe (2.08)
B	d1preb2	Membrane and cell surface proteins and peptides	Aerolisin/ETX pore-forming domain	Aerolisin/ETX pore-forming domain	(Pro)aerolysin, pore-forming lobe	(Pro)aerolysin, pore-forming lobe	(Aeromonas hydrophila ) [TaxId: 644 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	C-type lectin-like	8035141	3001261	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Aerolisin/ETX/LSL pore-forming domain-like	8035143	3000278	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aerolisin/ETX/LSL pore-forming domain-like	8035143	3000278	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	C-type lectin-like	8035141	3001261	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Aerolysin	e1preA1	A: beta complex topology	X: Aerolysin family of pore-forming toxins (From Topology)	H: Aerolysin family of pore-forming toxins (From Topology)	T: Aerolysin family of pore-forming toxins	F: Aerolysin	ECOD (1.6)
A	APT	e1preA2	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: C-type lectin-like	F: APT	ECOD (1.6)
B	Aerolysin	e1preB1	A: beta complex topology	X: Aerolysin family of pore-forming toxins (From Topology)	H: Aerolysin family of pore-forming toxins (From Topology)	T: Aerolysin family of pore-forming toxins	F: Aerolysin	ECOD (1.6)
B	APT	e1preB2	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: C-type lectin-like	F: APT	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.40.10	Alpha Beta	Roll	Pertussis Toxin	Chain B, domain 1	CATH (4.3.0)
A	3.30.412.10	Alpha Beta	2-Layer Sandwich	Proaerolysin	Chain A, domain 2	CATH (4.3.0)
A	2.170.15.10	Mainly Beta	Beta Complex	Proaerolysin	Chain A, domain 3	CATH (4.3.0)
B	3.10.40.10	Alpha Beta	Roll	Pertussis Toxin	Chain B, domain 1	CATH (4.3.0)
B	3.30.412.10	Alpha Beta	2-Layer Sandwich	Proaerolysin	Chain A, domain 2	CATH (4.3.0)
B	2.170.15.10	Mainly Beta	Beta Complex	Proaerolysin	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01117	Aerolysin toxin (Aerolysin)	Aerolysin toxin	This family represents the pore forming lobe of aerolysin.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROAEROLYSIN	identical protein binding protein binding binding toxin activity	-	cellular anatomical structure membrane host cell plasma membrane host cellular component host cell part host cell membrane extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR005831	Aerolysin/haemolysin toxin, conserved site	Conserved Site
A, B	IPR005830	Aerolysin	Family
A, B	IPR005138	Aerolysin/Pertussis toxin domain	Domain
A, B	IPR016187	C-type lectin fold	Homologous Superfamily
A, B	IPR037015	Aerolysin/Pertussis toxin (APT), N-terminal domain superfamily	Homologous Superfamily

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.