Annotations: 5O5Q

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03668	e5o5qA2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF03668	ECOD (1.6)
A	PF22740	e5o5qA1	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PF22740	ECOD (1.6)
B	PF03668	e5o5qB1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF03668	ECOD (1.6)
B	PF22740	e5o5qB2	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PF22740	ECOD (1.6)
C [auth D]	PF03668	e5o5qD2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF03668	ECOD (1.6)
C [auth D]	PF22740	e5o5qD1	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PF22740	ECOD (1.6)
D [auth C]	PF03668	e5o5qC2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF03668	ECOD (1.6)
D [auth C]	PF22740	e5o5qC1	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PF22740	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C [auth D], D [auth C]	PF03668	P-loop ATPase protein family (ATP_bind_2)	P-loop ATPase protein family	This family contains an ATP-binding site and could be an ATPase (personal obs:C Yeats).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C [auth D], D [auth C]	RNase adapter protein RapZ	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding molecular adaptor activity RNA binding nucleic acid binding guanyl nucleotide binding GTP binding guanyl ribonucleotide binding identical protein binding protein binding	protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis catabolic process regulation of cellular process cellular biosynthetic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis catabolic process regulation of cellular process cellular biosynthetic process positive regulation of biological process RNA metabolic process macromolecule catabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process positive regulation of metabolic process post-transcriptional regulation of gene expression regulation of RNA metabolic process organic substance metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process regulation of biological quality RNA catabolic process regulation of biosynthetic process RNA destabilization positive regulation of nucleobase-containing compound metabolic process regulation of biological process cellular metabolic process biological regulation primary metabolic process regulation of cellular metabolic process regulation of macromolecule metabolic process regulation of catabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process organic cyclic compound catabolic process nucleobase-containing compound catabolic process positive regulation of RNA metabolic process positive regulation of catabolic process regulation of cellular biosynthetic process organic cyclic compound metabolic process regulation of gene expression biosynthetic process regulation of RNA stability nucleic acid catabolic process metabolic process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of metabolic process organic substance catabolic process	protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C [auth D], D [auth C]	IPR005337	RapZ-like family	Family
A, B, C [auth D], D [auth C]	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.