Annotations: 3EE6

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF09286	e3ee6A4	A: a+b two layers	X: Alpha-beta plaits	H: Protease propeptides/inhibitors (From Topology)	T: Protease propeptides/inhibitors	F: PF09286	ECOD (1.6)
A	PF00082	e3ee6A3	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)
B	PF09286	e3ee6B4	A: a+b two layers	X: Alpha-beta plaits	H: Protease propeptides/inhibitors (From Topology)	T: Protease propeptides/inhibitors	F: PF09286	ECOD (1.6)
B	PF00082	e3ee6B3	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
B	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00082	Subtilase family (Peptidase_S8)	Subtilase family	Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7 ...	Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.	Domain
A, B	PF09286	Pro-kumamolisin, activation domain (Pro-kuma_activ)	Pro-kumamolisin, activation domain	Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Tripeptidyl-peptidase 1	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity binding ion binding anion binding phospholipid binding lipid binding lysophosphatidic acid binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity binding ion binding anion binding phospholipid binding lipid binding lysophosphatidic acid binding carbohydrate derivative binding small molecule binding serine-type exopeptidase activity exopeptidase activity tripeptidyl-peptidase activity peptide binding sulfatide binding glycolipid binding cation binding metal ion binding	cellular catabolic process organic substance metabolic process catabolic process cellular metabolic process metabolic process cellular process organic substance catabolic process peptide metabolic process peptide catabolic process developmental process multicellular organism development multicellular organismal process central nervous system development anatomical structure development cellular catabolic process organic substance metabolic process catabolic process cellular metabolic process metabolic process cellular process organic substance catabolic process peptide metabolic process peptide catabolic process developmental process multicellular organism development multicellular organismal process central nervous system development anatomical structure development nervous system development system development organonitrogen compound catabolic process organonitrogen compound metabolic process primary metabolic process protein catabolic process macromolecule catabolic process protein metabolic process macromolecule metabolic process epithelium development cellular developmental process cell differentiation tissue development epithelial cell differentiation lipid metabolic process system process nervous system process neuromuscular process neuromuscular process controlling balance cellular component organization lysosome organization organelle organization vacuole organization lytic vacuole organization cellular component organization or biogenesis protein localization localization cellular localization protein localization to chromosome protein localization to organelle cellular macromolecule localization macromolecule localization protein localization to chromosome, telomeric region protein catabolic process in the vacuole lysosomal protein catabolic process proteolysis multicellular organismal-level homeostasis homeostatic process tissue remodeling bone remodeling anatomical structure homeostasis tissue homeostasis bone resorption	membrane-bounded organelle intracellular anatomical structure pigment granule intracellular vesicle cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle melanosome cytoplasmic vesicle organelle cytoplasm vesicle lytic vacuole membrane-enclosed lumen membrane-bounded organelle intracellular anatomical structure pigment granule intracellular vesicle cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle melanosome cytoplasmic vesicle organelle cytoplasm vesicle lytic vacuole membrane-enclosed lumen vacuolar lumen vacuole lysosomal lumen intracellular organelle lumen organelle lumen lysosome extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space extracellular membrane-bounded organelle membrane microdomain membrane raft membrane Golgi apparatus endomembrane system endosome recycling endosome

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR030400	Sedolisin domain	Domain
A, B	IPR015366	Peptidase S53, activation domain	Domain
A, B	IPR000209	Peptidase S8/S53 domain	Domain
A, B	IPR036852	Peptidase S8/S53 domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: O14773	neuronal ceroid lipofuscinosis autosomal recessive spinocerebellar ataxia 7 Alzheimer disease neuronal ceroid lipofuscinosis 2 prostate cancer autosomal dominant cerebellar ataxia Ceroid Lipofuscinosis, Neuronal, 2 inborn errors of metabolism juvenile neuronal ceroid lipofuscinosis malignant ependymoma myopathy ovarian cancer pilocytic astrocytoma astrocytic tumor congenital neuronal ceroid lipofuscinosis neuronal ceroid lipofuscinosis autosomal recessive spinocerebellar ataxia 7 Alzheimer disease neuronal ceroid lipofuscinosis 2 prostate cancer autosomal dominant cerebellar ataxia Ceroid Lipofuscinosis, Neuronal, 2 inborn errors of metabolism juvenile neuronal ceroid lipofuscinosis malignant ependymoma myopathy ovarian cancer pilocytic astrocytoma astrocytic tumor congenital neuronal ceroid lipofuscinosis hereditary ataxia infantile neuronal ceroid lipofuscinosis malignant glioma neurodegenerative disease neuronal ceroid lipofuscinosis 4B adult neuronal ceroid lipofuscinosis peripheral nervous system disease polycystic ovary syndrome Down syndrome intellectual disability lysosomal storage disease medulloblastoma oligodendroglioma peripheral neuropathy atypical teratoid rhabdoid tumor tuberculosis epilepsy glioblastoma

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.