Annotations: 2YDQ

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Hyaluronidase post-catalytic domain-like	8038622	3001475	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	beta-N-acetylhexosaminidase-like domain	8038626	3000192	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	(Trans)glycosidases	8038623	3000313	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	NagJ_C	e2ydqA9	A: alpha bundles	X: Hyaluronidase domain-like	H: Hyaluronidase post-catalytic domain-like (From Topology)	T: Hyaluronidase post-catalytic domain-like	F: NagJ_C	ECOD (1.6)
A	NAGidase	e2ydqA8	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: NAGidase	ECOD (1.6)
A	Glyco_hydro_20b	e2ydqA7	A: mixed a+b and a/b	X: Zincin-like	H: beta-N-acetylhexosaminidase-like domain (From Topology)	T: beta-N-acetylhexosaminidase-like domain	F: Glyco_hydro_20b	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.379.10	Alpha Beta	2-Layer Sandwich	Chitobiase	domain 2	CATH (4.3.0)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
A	1.20.58.460	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21774	Hyaluronidase post-catalytic domain-like (NagJ_C)	Hyaluronidase post-catalytic domain-like	This domain is located at the C-terminus of proteins that are members of family 84 glycoside hydrolases.These enzymes directly hydrolyse O-GlcNAcylated peptides/proteins. This domain folds into a five helical bundle with up-and-down topology. It may ...	This domain is located at the C-terminus of proteins that are members of family 84 glycoside hydrolases.These enzymes directly hydrolyse O-GlcNAcylated peptides/proteins. This domain folds into a five helical bundle with up-and-down topology. It may function in substrate binding or recognition [1-5].	Domain
A	PF02838	Glycosyl hydrolase family 20, domain 2 (Glyco_hydro_20b)	Glycosyl hydrolase family 20, domain 2	This domain has a zincin-like fold.	Domain
A	PF07555	beta-N-acetylglucosaminidase (NAGidase)	beta-N-acetylglucosaminidase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	O-GLCNACASE NAGJ	binding carbohydrate binding hydrolase activity, acting on glycosyl bonds hexosaminidase activity beta-N-acetylhexosaminidase activity beta-N-acetylglucosaminidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity catalytic activity, acting on a protein	carbohydrate metabolic process primary metabolic process metabolic process macromolecule modification protein deglycosylation carbohydrate derivative metabolic process protein metabolic process macromolecule metabolic process protein modification process glycoprotein metabolic process polysaccharide metabolic process catabolic process polysaccharide catabolic process carbohydrate catabolic process carbohydrate metabolic process primary metabolic process metabolic process macromolecule modification protein deglycosylation carbohydrate derivative metabolic process protein metabolic process macromolecule metabolic process protein modification process glycoprotein metabolic process polysaccharide metabolic process catabolic process polysaccharide catabolic process carbohydrate catabolic process macromolecule catabolic process	-
B [auth T]	BIFUNCTIONAL PROTEIN NCOAT	hydrolase activity, acting on glycosyl bonds hexosaminidase activity beta-N-acetylhexosaminidase activity beta-N-acetylglucosaminidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity catalytic activity, acting on a protein hyalurononglucosaminidase activity identical protein binding protein binding binding	macromolecule modification protein deglycosylation carbohydrate derivative metabolic process metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process glycoprotein metabolic process carbohydrate derivative catabolic process glycoprotein catabolic process catabolic process protein catabolic process macromolecule catabolic process macromolecule modification protein deglycosylation carbohydrate derivative metabolic process metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process glycoprotein metabolic process carbohydrate derivative catabolic process glycoprotein catabolic process catabolic process protein catabolic process macromolecule catabolic process carbohydrate derivative biosynthetic process cellular biosynthetic process cellular metabolic process glycoprotein biosynthetic process protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule glycosylation protein O-linked glycosylation cellular process amino sugar metabolic process N-acetylglucosamine metabolic process glucosamine-containing compound metabolic process	membrane cellular anatomical entity intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR051822	Glycosyl Hydrolase Family 84	Family
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR003961	Fibronectin type III	Domain
A	IPR029018	Beta-hexosaminidase-like, domain 2	Homologous Superfamily
A	IPR011496	Beta-N-acetylglucosaminidase, catalytic domain	Domain
A	IPR008965	CBM2/CBM3, carbohydrate-binding domain superfamily	Homologous Superfamily
A	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A	IPR002102	Cellulosome anchoring protein, cohesin domain	Domain
A	IPR000421	Coagulation factor 5/8, C-terminal domain	Domain
A	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A	IPR015882	Beta-hexosaminidase, bacterial type, N-terminal	Domain
A	IPR049019	NagJ-like, helical domain	Domain
A	IPR036116	Fibronectin type III superfamily	Homologous Superfamily
B [auth T]	IPR051822	Glycosyl Hydrolase Family 84	Family
B [auth T]	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
B [auth T]	IPR011496	Beta-N-acetylglucosaminidase, catalytic domain	Domain
B [auth T]	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
B [auth T]	Pharos: O60502	pancreatic intraductal papillary-mucinous neoplasm subependymal giant cell astrocytoma adrenal cortex carcinoma atrial fibrillation glioblastoma large cell medulloblastoma malignant pancreatic neoplasm oligodendroglioma pancreatic ductal adenocarcinoma Pick disease tuberculosis amyotrophic lateral sclerosis dermatomyositis juvenile dermatomyositis malignant ependymoma pancreatic intraductal papillary-mucinous neoplasm subependymal giant cell astrocytoma adrenal cortex carcinoma atrial fibrillation glioblastoma large cell medulloblastoma malignant pancreatic neoplasm oligodendroglioma pancreatic ductal adenocarcinoma Pick disease tuberculosis amyotrophic lateral sclerosis dermatomyositis juvenile dermatomyositis malignant ependymoma medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous carcinoma psoriasis astrocytic tumor Emery-Dreifuss muscular dystrophy kidney disease malignant glioma myopathy ovarian cancer

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.