Annotations: 1ZTF

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	RIO1	e1ztfA1	A: a+b complex topology	X: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)	H: Protein kinase/SAICAR synthase/ATP-grasp	T: Protein kinase	F: RIO1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01163	RIO domain (RIO1)	RIO domain	This is the atypical serine kinase domain found in RIO family of proteins and related sequences, which is conserved in archaea, bacteria and eukaryotes [5,6]. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, ...	This is the atypical serine kinase domain found in RIO family of proteins and related sequences, which is conserved in archaea, bacteria and eukaryotes [5,6]. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined [4]. This domain is also found at the C-terminal of EKC/KEOPS complex subunit BUD32 from Fungi and Kae1/Bud32 from archaea [6].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Rio1 serine protein kinase	protein serine/threonine kinase activity catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity histone H3S57 kinase activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups histone H3 kinase activity histone modifying activity catalytic activity histone kinase activity histone H2AS121 kinase activity histone H2A kinase activity protein serine/threonine kinase activity catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity histone H3S57 kinase activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups histone H3 kinase activity histone modifying activity catalytic activity histone kinase activity histone H2AS121 kinase activity histone H2A kinase activity Rho-dependent protein serine/threonine kinase activity AMP-activated protein kinase activity histone H2AT120 kinase activity hydrolase activity DNA-dependent protein kinase activity histone H3T45 kinase activity histone H2AXS139 kinase activity histone H2AX kinase activity histone H4S1 kinase activity histone H4 kinase activity protein serine kinase activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding histone H3T11 kinase activity histone H3S28 kinase activity histone H3T6 kinase activity 3-phosphoinositide-dependent protein kinase activity histone H2B kinase activity histone H2BS36 kinase activity histone H3T3 kinase activity histone H2AS1 kinase activity ribosomal protein S6 kinase activity histone H3S10 kinase activity cation binding metal ion binding histone H2BS14 kinase activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018935	RIO kinase, conserved site	Conserved Site
A	IPR000719	Protein kinase domain	Domain
A	IPR000687	RIO kinase	Domain
A	IPR011009	Protein kinase-like domain superfamily	Homologous Superfamily
A	IPR051272	RIO-type Ser/Thr kinase	Family
A	IPR018934	RIO-type domain	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 R01GM157729.