3ENH

Crystal structure of Cgi121/Bud32/Kae1 complex

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Protein kinase-like (PK-like)	8058158	3000066	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Actin-like ATPases	8092403	3000092	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Actin-like ATPases	8058156	3000092	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Protein kinase-like (PK-like)	8058158	3000066	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Actin-like ATPases	8058156	3000092	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Actin-like ATPases	8092403	3000092	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	RIO1	e3enhA5	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)
A	Peptidase_M22_C_1	e3enhA3	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Peptidase_M22_C_1	ECOD (1.6)
A	Peptidase_M22_N	e3enhA4	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Peptidase_M22_N	ECOD (1.6)
B	RIO1	e3enhB5	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)
B	Peptidase_M22_C_1	e3enhB3	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Peptidase_M22_C_1	ECOD (1.6)
B	Peptidase_M22_N	e3enhB4	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Peptidase_M22_N	ECOD (1.6)
C	CGI-121	e3enhC1	A: a+b two layers	X: Alpha-beta plaits	H: PF0523-like (From Topology)	T: PF0523-like	F: CGI-121	ECOD (1.6)
D	CGI-121	e3enhD1	A: a+b two layers	X: Alpha-beta plaits	H: PF0523-like (From Topology)	T: PF0523-like	F: CGI-121	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
A	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
A	1.10.510.10	Mainly Alpha	Orthogonal Bundle	Transferase(Phosphotransferase)	domain 1	CATH (4.3.0)
B	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
B	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
B	1.10.510.10	Mainly Alpha	Orthogonal Bundle	Transferase(Phosphotransferase)	domain 1	CATH (4.3.0)
C	3.30.2380.10	Alpha Beta	2-Layer Sandwich	PF0523-like	CGI121/TPRKB	CATH (4.3.0)
D	3.30.2380.10	Alpha Beta	2-Layer Sandwich	PF0523-like	CGI121/TPRKB	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00814	tRNA N6-adenosine threonylcarbamoyltransferase (TsaD)	tRNA N6-adenosine threonylcarbamoyltransferase	-	Family
A, B	PF01163	RIO1 family (RIO1)	RIO1 family	-	Family
C, D	PF08617	Kinase binding protein CGI-121 (CGI-121)	Kinase binding protein CGI-121	CGI-121 has been shown to bind to the p53-related protein kinase (PRPK) [1]. PRPK is a novel protein kinase which binds to and induces phosphorylation of the tumour suppressor protein p53. CGI-121 is part of a conserved protein complex, KEOPS. The K ...	CGI-121 has been shown to bind to the p53-related protein kinase (PRPK) [1]. PRPK is a novel protein kinase which binds to and induces phosphorylation of the tumour suppressor protein p53. CGI-121 is part of a conserved protein complex, KEOPS. The KEOPS complex is involved in telomere uncapping and telomere elongation [2]. Interestingly this family also include archaeal homologues, formerly in the DUF509 family. A structure for these proteins has been solved by structural genomics.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Putative O-sialoglycoprotein endopeptidase	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 protein serine/threonine/tyrosine kinase activity catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups protein serine/threonine kinase activity cation binding transition metal ion binding iron ion binding metal ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity endopeptidase activity zinc ion binding acyltransferase activity N(6)-L-threonylcarbamoyladenine synthase activity acyltransferase activity, transferring groups other than amino-acyl groups protein serine kinase activity	tRNA threonylcarbamoyladenosine modification tRNA modification RNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process RNA modification biosynthetic process tRNA processing tRNA threonylcarbamoyladenosine modification tRNA modification RNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process RNA modification biosynthetic process tRNA processing macromolecule modification tRNA threonylcarbamoyladenosine metabolic process metabolic process cellular process macromolecule metabolic process RNA processing	protein-containing complex catalytic complex transferase complex EKC/KEOPS complex cellular anatomical structure intracellular anatomical structure cytoplasm
C, D	Uncharacterized protein MJ0187	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR022495	Serine/threonine-protein kinase Bud32	Family
A, B	IPR017860	Peptidase M22, conserved site	Conserved Site
A, B	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
A, B	IPR008266	Tyrosine-protein kinase, active site	Active Site
A, B	IPR009220	Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein	Family
A, B	IPR011009	Protein kinase-like domain superfamily	Homologous Superfamily
A, B	IPR000905	Gcp-like domain	Domain
A, B	IPR034680	tRNA N6-adenosine threonylcarbamoyltransferase Kae1, archaeal/eukaryotic	Family
A, B	IPR017861	Kae1/TsaD family	Family
A, B	IPR000719	Protein kinase domain	Domain
C, D	IPR036504	CGI121/TPRKB superfamily	Homologous Superfamily
C, D	IPR013926	CGI121/TPRKB	Family

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.