Annotations: 1YSC

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ysca_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Serine carboxypeptidase II	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8033222	3000102	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	PF00450	e1yscA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00450	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
A	1.10.287.410	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00450	Serine carboxypeptidase (Peptidase_S10)	Serine carboxypeptidase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	SERINE CARBOXYPEPTIDASE	serine-type exopeptidase activity peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type carboxypeptidase activity serine-type peptidase activity hydrolase activity exopeptidase activity catalytic activity carboxypeptidase activity	cellular catabolic process catabolic process macroautophagy cellular metabolic process autophagy cellular process metabolic process process utilizing autophagic mechanism organonitrogen compound metabolic process organonitrogen compound biosynthetic process phytochelatin biosynthetic process amide biosynthetic process secondary metabolic process organic substance metabolic process cellular catabolic process catabolic process macroautophagy cellular metabolic process autophagy cellular process metabolic process process utilizing autophagic mechanism organonitrogen compound metabolic process organonitrogen compound biosynthetic process phytochelatin biosynthetic process amide biosynthetic process secondary metabolic process organic substance metabolic process biosynthetic process secondary metabolite biosynthetic process organic substance biosynthetic process amide metabolic process phytochelatin metabolic process zymogen activation cellular biosynthetic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation proteolysis protein processing protein metabolic process macromolecule metabolic process	membrane-bounded organelle storage vacuole intracellular anatomical structure lytic vacuole vacuole cellular anatomical entity intracellular membrane-bounded organelle fungal-type vacuole intracellular organelle organelle cytoplasm extracellular region membrane-enclosed lumen vacuolar lumen membrane-bounded organelle storage vacuole intracellular anatomical structure lytic vacuole vacuole cellular anatomical entity intracellular membrane-bounded organelle fungal-type vacuole intracellular organelle organelle cytoplasm extracellular region membrane-enclosed lumen vacuolar lumen intracellular organelle lumen organelle lumen fungal-type vacuole lumen endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001563	Peptidase S10, serine carboxypeptidase	Family
A	IPR018202	Serine carboxypeptidase, serine active site	Active Site
A	IPR008442	Propeptide, carboxypeptidase Y	Domain
A	IPR033124	Serine carboxypeptidases, histidine active site	Active Site
A	IPR029058	Alpha/Beta hydrolase fold	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 R01GM133198.