4TF4

ENDO/EXOCELLULASE:CELLOPENTAOSE FROM THERMOMONOSPORA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4tf4a1	All alpha proteins	alpha/alpha toroid	Six-hairpin glycosidases	Cellulases catalytic domain	Endo/exocellulase:cellobiose E-4, N-terminal domain	(Thermobifida fusca ) [TaxId: 2021 ],	SCOPe (2.08)
A	d4tf4a2	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Carbohydrate-binding domain	Cellulose-binding domain family III	Endo/exocellulase:cellobiose E-4, C-terminal domain	(Thermobifida fusca ) [TaxId: 2021 ],	SCOPe (2.08)
B	d4tf4b1	All alpha proteins	alpha/alpha toroid	Six-hairpin glycosidases	Cellulases catalytic domain	Endo/exocellulase:cellobiose E-4, N-terminal domain	(Thermobifida fusca ) [TaxId: 2021 ],	SCOPe (2.08)
B	d4tf4b2	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Carbohydrate-binding domain	Cellulose-binding domain family III	Endo/exocellulase:cellobiose E-4, C-terminal domain	(Thermobifida fusca ) [TaxId: 2021 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Carbohydrate-binding domain	8040189	3000706	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Six-hairpin glycosidases	8038371	3000970	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Six-hairpin glycosidases	8038371	3000970	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Carbohydrate-binding domain	8040189	3000706	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	CBM_3	e4tf4A1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: CBM_3	ECOD (1.6)
A	Glyco_hydro_9	e4tf4A2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_9	ECOD (1.6)
B	CBM_3	e4tf4B1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: CBM_3	ECOD (1.6)
B	Glyco_hydro_9	e4tf4B2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_9	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)
A	2.60.40.710	Mainly Beta	Sandwich	Immunoglobulin-like	Endoglucanase-like	CATH (4.3.0)
B	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)
B	2.60.40.710	Mainly Beta	Sandwich	Immunoglobulin-like	Endoglucanase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00942	Cellulose binding domain (CBM_3)	Cellulose binding domain	-	Domain
A, B	PF00759	Glycosyl hydrolase family 9 (Glyco_hydro_9)	Glycosyl hydrolase family 9	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	T. FUSCA ENDO/EXO-CELLULASE E4 CATALYTIC DOMAIN AND CELLULOSE-BINDING DOMAIN	hydrolase activity, acting on glycosyl bonds cellulase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity binding polysaccharide binding cellulose binding carbohydrate binding	carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellulose catabolic process macromolecule metabolic process carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellulose catabolic process macromolecule metabolic process cellulose metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR012291	CBM2, carbohydrate-binding domain superfamily	Homologous Superfamily
A, B	IPR036966	Carbohydrate-binding module 3 superfamily	Homologous Superfamily
A, B	IPR001956	Carbohydrate-binding module 3	Domain
A, B	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
A, B	IPR003961	Fibronectin type III	Domain
A, B	IPR018366	Carbohydrate-binding type-2, conserved site	Conserved Site
A, B	IPR008965	CBM2/CBM3, carbohydrate-binding domain superfamily	Homologous Superfamily
A, B	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A, B	IPR018221	Glycoside hydrolase family 9, His active site	Active Site
A, B	IPR033126	Glycosyl hydrolases family 9, Asp/Glu active sites	Active Site
A, B	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A, B	IPR001701	Glycoside hydrolase family 9	Domain
A, B	IPR001919	Carbohydrate-binding type-2 domain	Domain
A, B	IPR036116	Fibronectin type III superfamily	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.