2BWB

Crystal structure of the UBA domain of Dsk2 from S. cerevisiae

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d2bwba_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
B	d2bwbb_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
C	d2bwbc_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
D	d2bwbd_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
E	d2bwbe_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
F	d2bwbf_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
G	d2bwbg_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
H	d2bwbh_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
I	d2bwbi_	All alpha proteins	RuvA C-terminal domain-like	UBA-like	UBA domain	automated matches	(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	SCOP2 Family	UBA domain	8026360	4000749	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	UBA-like	8038739	3001235	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	UBA-like	8038739	3001235	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	UBA-like	8038739	3001235	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	PF00627	e2bwbA1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
B	PF00627	e2bwbB1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
C	PF00627	e2bwbC1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
D	PF00627	e2bwbD1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
E	PF00627	e2bwbE1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
F	PF00627	e2bwbF1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
G	PF00627	e2bwbG1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
H	PF00627	e2bwbH1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)
I	PF00627	e2bwbI1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: PF00627	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
B	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
C	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
D	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
E	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
F	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
G	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
H	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
I	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I	UBIQUITIN-LIKE PROTEIN DSK2	polyubiquitin modification-dependent protein binding protein binding binding modification-dependent protein binding protein-macromolecule adaptor activity molecular adaptor activity	protein localization localization cellular localization protein localization to organelle cellular macromolecule localization macromolecule localization protein localization to vacuole cellular process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process protein localization localization cellular localization protein localization to organelle cellular macromolecule localization macromolecule localization protein localization to vacuole cellular process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process spindle pole body duplication microtubule organizing center organization microtubule cytoskeleton organization cellular component organization cellular component biogenesis organelle organization cellular component assembly spindle pole body organization microtubule-based process cell cycle cellular component organization or biogenesis cytoskeleton organization cell cycle process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR019954	Ubiquitin conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR000626	Ubiquitin-like domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR015496	Ubiquilin	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR029071	Ubiquitin-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR009060	UBA-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR015940	Ubiquitin-associated domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR006636	Heat shock chaperonin-binding	Domain

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.