Annotations: 5A9X

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03144	e5a9xA2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: PF03144	ECOD (1.6)
A	F_UNCLASSIFIED	e5a9xA5	A: a+b two layers	X: Alpha-beta plaits	H: EF-G C-terminal domain-like (From Topology)	T: EF-G C-terminal domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF00679	e5a9xA1	A: a+b two layers	X: Alpha-beta plaits	H: EF-G C-terminal domain-like (From Topology)	T: EF-G C-terminal domain-like	F: PF00679	ECOD (1.6)
A	PF21018	e5a9xA4	A: a+b complex topology	X: C-terminal domain of BipA (From Topology)	H: C-terminal domain of BipA (From Topology)	T: C-terminal domain of BipA	F: PF21018	ECOD (1.6)
A	PF00009	e5a9xA3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00009	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00679	Elongation factor G C-terminus (EFG_C)	Elongation factor G C-terminus	This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.	Domain
A	PF00009	Elongation factor Tu GTP binding domain (GTP_EFTU)	Elongation factor Tu GTP binding domain	This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.	Domain
A	PF03144	Elongation factor Tu domain 2 (GTP_EFTU_D2)	Elongation factor Tu domain 2	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.	Domain
A	PF21018	TypA/BipA C-terminal domain (BipA_C)	TypA/BipA C-terminal domain	This entry represents the C-terminal domain of the TypA/BipA protein. The C-terminal domain of BipA, consisting of residues, forms a unique motif with two crossed beta sheets (comprising of two and four beta-strands, respectively) wrapped by three sh ...	This entry represents the C-terminal domain of the TypA/BipA protein. The C-terminal domain of BipA, consisting of residues, forms a unique motif with two crossed beta sheets (comprising of two and four beta-strands, respectively) wrapped by three short alpha helices forming a nearly equilateral triangle [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	GTP-BINDING PROTEIN	guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding RNA binding rRNA binding nucleic acid binding ribonucleoprotein complex binding protein-containing complex binding ribosome binding tRNA binding GTP binding purine ribonucleoside triphosphate binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	cellular component biogenesis ribosome biogenesis ribonucleoprotein complex biogenesis cellular process cellular component organization or biogenesis	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000795	Translational (tr)-type GTP-binding domain	Domain
A	IPR000640	Elongation factor EFG, domain V-like	Domain
A	IPR047043	GTP-binding protein BipA, domain 3	Domain
A	IPR031157	Tr-type G domain, conserved site	Conserved Site
A	IPR035647	EF-G domain III/V-like	Homologous Superfamily
A	IPR047041	GTP-binding protein BipA, GTP-binding domain	Domain
A	IPR006298	GTP-binding protein BipA	Family
A	IPR042116	GTP-binding protein TypA/BipA, C-terminal	Homologous Superfamily
A	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
A	IPR047042	GTP-binding protein BipA, domain 2	Domain
A	IPR035651	BipA, domain V	Domain
A	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
A	IPR005225	Small GTP-binding protein domain	Domain
A	IPR048876	TypA/BipA, C-terminal domain	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	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.