Annotations: 1YBY

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ybya1	All beta proteins	SH3-like barrel	Translation proteins SH3-like domain	automated matches	automated matches	(Acetivibrio thermocellus ) [TaxId: 1515 ],	SCOPe (2.08)
A	d1ybya2	All beta proteins	OB-fold	Nucleic acid-binding proteins	automated matches	automated matches	(Acetivibrio thermocellus ) [TaxId: 1515 ],	SCOPe (2.08)
B	d1ybyb1	All beta proteins	SH3-like barrel	Translation proteins SH3-like domain	automated matches	automated matches	(Acetivibrio thermocellus ) [TaxId: 1515 ],	SCOPe (2.08)
B	d1ybyb2	All beta proteins	OB-fold	Nucleic acid-binding proteins	automated matches	automated matches	(Acetivibrio thermocellus ) [TaxId: 1515 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EFP	e1ybyA1	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: EFP	ECOD (1.6)
A	Elong-fact-P_C	e1ybyA2	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: Elong-fact-P_C	ECOD (1.6)
A	EFP_N	e1ybyA3	A: beta barrels	X: SH3	H: SH3	T: SH3	F: EFP_N	ECOD (1.6)
B	EFP	e1ybyB4	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: EFP	ECOD (1.6)
B	Elong-fact-P_C	e1ybyB6	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: Elong-fact-P_C	ECOD (1.6)
B	EFP_N	e1ybyB5	A: beta barrels	X: SH3	H: SH3	T: SH3	F: EFP_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.30.30	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
A	2.40.50.140	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	Nucleic acid-binding proteins	CATH (4.3.0)
B	2.30.30.30	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
B	2.40.50.140	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	Nucleic acid-binding proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF09285	Elongation factor P, C-terminal (Elong-fact-P_C)	Elongation factor P, C-terminal	Members of this family of nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology [1].	Domain
A, B	PF01132	Elongation factor P (EF-P) OB domain (EFP)	Elongation factor P (EF-P) OB domain	-	Domain
A, B	PF08207	Elongation factor P (EF-P) KOW-like domain (EFP_N)	Elongation factor P (EF-P) KOW-like domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Translation elongation factor P	translation regulator activity binding organic cyclic compound binding translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding	-	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011768	Translation elongation factor P	Family
A, B	IPR020599	Translation elongation factor P/YeiP	Family
A, B	IPR015365	Elongation factor P, C-terminal	Domain
A, B	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily
A, B	IPR013185	Translation elongation factor, KOW-like	Domain
A, B	IPR014722	Large ribosomal subunit protein uL2, domain 2	Homologous Superfamily
A, B	IPR013852	Translation elongation factor P/YeiP, conserved site	Conserved Site
A, B	IPR008991	Translation protein SH3-like domain superfamily	Homologous Superfamily
A, B	IPR001059	Translation elongation factor P/YeiP, central	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.