Annotations: 7DIA

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	M16C_assoc	e7diaA1	A: a+b two layers	X: LuxS, MPP, ThrRS/AlaRS common domain	H: LuxS, MPP, ThrRS/AlaRS common domain	T: LuxS/MPP-like metallohydrolase	F: M16C_assoc	ECOD (1.6)
A	Peptidase_M16_C_4	e7diaA4	A: a+b two layers	X: LuxS, MPP, ThrRS/AlaRS common domain	H: LuxS, MPP, ThrRS/AlaRS common domain	T: LuxS/MPP-like metallohydrolase	F: Peptidase_M16_C_4	ECOD (1.6)
A	Peptidase_M16_C_3	e7diaA2	A: a+b two layers	X: LuxS, MPP, ThrRS/AlaRS common domain	H: LuxS, MPP, ThrRS/AlaRS common domain	T: LuxS/MPP-like metallohydrolase	F: Peptidase_M16_C_3	ECOD (1.6)
A	Peptidase_M16	e7diaA3	A: a+b two layers	X: LuxS, MPP, ThrRS/AlaRS common domain	H: LuxS, MPP, ThrRS/AlaRS common domain	T: LuxS/MPP-like metallohydrolase	F: Peptidase_M16	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05193	Peptidase M16 inactive domain (Peptidase_M16_C)	Peptidase M16 inactive domain	Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp [1].	Domain
A	PF08367	Peptidase M16C associated (M16C_assoc)	Peptidase M16C associated	-	Family
A	PF22516	PreP C-terminal domain (PreP_C)	PreP C-terminal domain	PreP is a protease that degrades targeting peptides as well as other unstructured peptides in both mitochondria and chloroplasts. This entry represents the C-terminal domain of PreP and related proteins.	Domain
A	PF00675	Insulinase (Peptidase family M16) (Peptidase_M16)	Insulinase (Peptidase family M16)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Falcilysin	cation binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity	catabolic process metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process hemoglobin metabolic process hemoglobin catabolic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process catabolic process metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process hemoglobin metabolic process hemoglobin catabolic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process proteolysis protein processing	vacuolar membrane membrane-bounded organelle intracellular anatomical structure membrane vacuole intracellular membrane-bounded organelle intracellular organelle bounding membrane of organelle cellular anatomical structure organelle cytoplasm organelle membrane plastid apicoplast vacuolar membrane membrane-bounded organelle intracellular anatomical structure membrane vacuole intracellular membrane-bounded organelle intracellular organelle bounding membrane of organelle cellular anatomical structure organelle cytoplasm organelle membrane plastid apicoplast phagolysosome lytic vacuole intracellular vesicle phagocytic vesicle food vacuole cytoplasmic vesicle secondary lysosome vesicle endocytic vesicle lysosome

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR007863	Peptidase M16, C-terminal	Domain
A	IPR055130	Presequence protease, mitochondrial-type, C-terminal domain	Domain
A	IPR011765	Peptidase M16, N-terminal	Domain
A	IPR013578	Peptidase M16C associated	Domain
A	IPR011249	Metalloenzyme, LuxS/M16 peptidase-like	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.