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EC Tree
IUBMB Comments This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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a [protein]-(L-serine/L-threonine)
=
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a [protein]-(L-serine/L-threonine) phosphate
Synonyms
protein kinase a, 14-3-3, camkii, p-akt, lrrk2, c-jun n-terminal kinase, serine/threonine kinase, raf-1, protein kinase b, gsk-3,
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A-T, mutated homolog
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AMH type II receptor
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Anti-sigma B factor rsbT
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Ataxia telangiectasia mutated
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Ataxia telangiectasia mutated homolog
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ATP-protein transphosphorylase
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Breast-tumor-amplified kinase
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Calcium-dependent protein kinase C
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Calcium/phospholipid-dependent protein kinase
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cAMP-dependent protein kinase A
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CDC25 suppressing protein kinase
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Cell division cycle 2-like
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CLP-36 interacting kinase
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cyclic monophosphate-dependent protein kinase
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cyclic nucleotide-dependent protein kinase
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cyclin-dependent kinase
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cytidine 3',5'-cyclic monophosphate-responsive protein kinase
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hydroxyalkyl-protein kinase
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Kinase interacting with stathmin
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kinase, casein (phosphorylating)
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kinase, protamine (phosphorylating)
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kinase, protein (phosphorylating)
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kinase, protein, A (phosphorylating)
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kinase, protein, C (phosphorylating)
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Lymphocyte-oriented kinase
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M phase-specific cdc2 kinase
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mitogen-activated S6 kinase
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Myristoylated and palmitoylated serine-threonine kinase
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NY-REN-55 antigen
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phosphorylase b kinase kinase
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Pre-mRNA protein kinase
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protein glutamyl kinase
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protein kinase (phosphorylating)
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Protein kinase B kinase
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protein kinase CK2
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Protein kinase Krct
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Protein kinase MST
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protein kinase p58
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Protein kinase PKL12
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protein phosphokinase
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protein serine kinase
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protein serine-threonine kinase
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protein-aspartyl kinase
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protein-cysteine kinase
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protein-serine kinase
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protein-serine/threonine kinase
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PRP4 pre-mRNA processing factor 4 homolog
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ribosomal protein S6 kinase II
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ribosomal S6 protein kinase
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RIO serine protein kinase
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S-receptor kinase
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serine protein kinase
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serine(threonine) protein kinase
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serine-specific protein kinase
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serine/threonine kinase
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Serine/threonine kinase 15
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Serine/threonine kinase Ayk1
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serine/threonine protein kinase
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Serine/threonine-protein kinase NRK2
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Serine/threonine-protein kinase NYD-SPK
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Ste20-like kinase
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STE20-like kinase MST1
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STE20-like kinase MST2
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STE20-like kinase MST3
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Switch protein/serine kinase
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threonine-specific protein kinase
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type-2 casein kinase
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additional information
the enzyme belongs to the Rio family, Rio2 subfamily, of serine/threonine protein kinases
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phospho group transfer
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ATP:protein phosphotransferase (non-specific)
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
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191808-15-8
phosphoinositide dependent protein kinase 1
377752-08-4
ribosomal protein S6 kinase 2
389133-24-8
ribosomal S6 kinase 3
52660-18-1
casein kinase, protein kinase CK2
9026-43-1
this CAS Reg. No. encompasses a great variety of protein kinases including the serine/threonine specific kinases
90698-26-3
ribosomal protein S6 kinase 1
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ATP + a protein
ADP + a phosphoprotein
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?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
dephosphorylated alpha-casein
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ATP + histone
ADP + phosphorylated histone
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ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
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additional information
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additional information
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kinase Rio2 is required for rRNA cleavage in 40S ribosomal subunit maturation
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additional information
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Rio2 performs autophosphorylation
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additional information
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kinase Rio2 is required for rRNA cleavage in 40S ribosomal subunit maturation
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ATP
binding structure involving residues K168, S53, and D166, overview
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ATP
substrate inhibition. At ATP concentrations above 0.1 mM, kinase activity begins to drop until at 100 mM it becomes almost unmeasurable
Toyocamycin
toyocamycin binds in the ATP binding pocket of the protein more tightly than ATP/Mg2+
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SwissProt
brenda
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physiological function
the enzyme is necessary for the final processing step of maturing the 18S ribosomal rRNA
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30100
x * 30100, calculated from sequence, autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity
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oligomer
x * 30100, calculated from sequence, autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity
additional information
the kinase domain is tightly connected to a wHTH domain
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phosphoprotein
Ser108 represents the sole autophosphorylation site of Aeroglobus fulgidus Rio1
phosphoprotein
Rio2 performs autophosphorylation
phosphoprotein
autophosphorylation at Ser128
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hanging drop vapor diffusion method, high resolution crystal structures of Archaeoglobus fulgidus Rio1 in the presence and absence of bound nucleotides
X-ray crystal structure of toyocamycin bound to Rio1 at 2.0 A, toyocamycin binds in the ATP binding pocket of the protein
hanging drop vapor diffusion in 1 ml wells containing 512% poly(ethylene glycol) 900 and 100 mM sodium phosphate/citrate buffer, pH 3.64.1. Crystallization of the enzyme after incubation with ATP or ADP and Mn2+. Co-crystal structures of Rio2ATPMn and Rio2ADPMn are solved at 1.84 and 1.75 A resolution, respectively
purified recombinant wild-type and selenomethionine-labeled Rio2, hanging drop vapour diffusion method, equal volumes of protein solution, containing 5-12% PEG 900, and 0.1 M phosphate citrate buffer, pH 3.6-4.1, and reservoir solution, versus 1 ml reservoir solution, purified recombinant Rio2 complexed with ATP using 0.1 M Tris, pH 7.5, 20 mM ATP, 20 mM MgCl2, 20 mM adenosine 5'-(beta,gamma-imino)triphosphate, and 20% ethylene glycol, 20°C, 2-4 days, X-ray diffraction structure determination and analysis at 2.0 A resolution
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76
Tm-value of unbound enzyme
88
Tm-value in presence of toyocamycin
82
Tm-value in presence of ATP and Mg2+
82
Tm-value in presence of sangivamycin
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recombinant Rio2 from Escherichia coli by adsorption chromatography and gel filtration
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expression in Escherichia coli
expression of Rio2 in Escherichia coli
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LaRonde-LeBlanc, N.; Wlodawer, A.
Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases
Structure
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1585-1594
2004
Archaeoglobus fulgidus (O30245)
brenda
LaRonde-LeBlanc, N.; Guszczynski, T.; Copeland, T.; Wlodawer, A.
Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes
FEBS J.
272
2800-2810
2005
Archaeoglobus fulgidus (O30245), Archaeoglobus fulgidus
brenda
Laronde-Leblanc, N.; Guszczynski, T.; Copeland, T.; Wlodawer, A.
Structure and activity of the atypical serine kinase Rio1
FEBS J.
272
3698-3713
2005
Archaeoglobus fulgidus (O28471), Archaeoglobus fulgidus
brenda
Kiburu, I.N.; LaRonde-LeBlanc, N.
Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity
PLoS ONE
7
e37371
2012
Archaeoglobus fulgidus (O28471), Archaeoglobus fulgidus
brenda
Transporter Classification Database (TCDB):
8.A.23.1.35 ,
9.B.321.1.1 ,
8.A.104.1.10 ,
1.A.87.2.4 ,
1.I.1.1.3 ,
1.A.87.2.9 ,
8.A.104.1.1 ,
1.A.87.2.6 ,
1.I.1.1.5 ,
9.A.15.1.1 ,
1.A.4.5.8 ,
1.A.4.5.1 ,
1.A.87.2.11 ,
8.A.104.1.9 ,
1.A.87.2.3 ,
8.A.104.1.5 ,
2.A.133.1.3