Annotations: 1J36

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1j36a1	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Neurolysin-like	Angiotensin converting enzyme, ACE	fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
A	d1j36a2	Artifacts	Tags	Tags	Tags	C-terminal Tags	fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
B	d1j36b1	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Neurolysin-like	Angiotensin converting enzyme, ACE	fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
B	d1j36b2	Artifacts	Tags	Tags	Tags	C-terminal Tags	fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Neurolysin-like	8019862	4001613	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Metalloproteases (zincins), catalytic domain	8032242	3001975	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8032242	3001975	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	Peptidase_M2	e1j36A1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M2	ECOD (1.6)
B	Peptidase_M2	e1j36B1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M2	ECOD (1.6)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	angiotensin converting enzyme	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity peptidyl-dipeptidase activity exopeptidase activity carboxypeptidase activity cation binding ion binding binding metal ion binding small molecule binding	sexual reproduction reproductive process developmental process multicellular organism development multicellular organismal process anatomical structure development metamorphosis peptide hormone processing cellular biosynthetic process regulation of hormone levels cellular metabolic process biological regulation signaling receptor ligand precursor processing primary metabolic process sexual reproduction reproductive process developmental process multicellular organism development multicellular organismal process anatomical structure development metamorphosis peptide hormone processing cellular biosynthetic process regulation of hormone levels cellular metabolic process biological regulation signaling receptor ligand precursor processing primary metabolic process gene expression macromolecule biosynthetic process hormone metabolic process protein maturation biosynthetic process proteolysis protein processing metabolic process cellular process amide metabolic process protein metabolic process macromolecule metabolic process regulation of biological quality response to symbiont biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to bacterium response to symbiotic bacterium response to external stimulus response to external biotic stimulus response to biotic stimulus	cell periphery plasma membrane membrane cellular anatomical entity extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001548	Peptidase M2, peptidyl-dipeptidase A	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.