O28471 (RIO1_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RIO-type serine/threonine-protein kinase Rio1
Short name=AfRio1
EC=2.7.11.1

Gene names

Name:	rio1
Ordered Locus Names:	AF_1804

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus › Archaeoglobus fulgidus

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Autophosphorylation of the rio1 protein is not necessary for maintenance of kinase activity. Prefers ATP over GTP. The yeast ortholog is involved in ribosome biogenesis.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Sequence similarities	Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 258

258

RIO-type serine/threonine-protein kinase Rio1

PRO_0000344796

Regions

Domain

49 – 258

210

Protein kinase

Nucleotide binding

55 – 63

9

ATP By similarity

Sites

Active site

196

1

Proton acceptor By similarity

Metal binding

201

1

Magnesium

Metal binding

212

1

Magnesium

Binding site

80

1

ATP

Binding site

148

1

ATP; via carbonyl oxygen

Binding site

150

1

ATP; via amide nitrogen

Binding site

201

1

ATP

Binding site

212

1

ATP

Amino acid modifications

Modified residue

108

1

Phosphoserine; by autocatalysis Ref.2

Experimental info

Mutagenesis

108

1

S → A: Absence of autophosphorylation, retains kinase activity. Ref.2

Mutagenesis

196

1

D → A: Drastically reduced kinase activity. Ref.2

Secondary structure

1

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258

Helix Strand Turn

Details...

Helix

4 – 13

10

Helix

18 – 20

3

Helix

23 – 30

8

Helix

33 – 44

12

Beta strand

47 – 57

11

Beta strand

59 – 70

12

Beta strand

73 – 82

10

Helix

93 – 95

3

Turn

96 – 98

3

Helix

104 – 106

3

Helix

110 – 129

20

Beta strand

137 – 141

5

Beta strand

144 – 148

5

Helix

160 – 163

4

Helix

164 – 169

6

Helix

172 – 188

17

Beta strand

192 – 194

3

Beta strand

201 – 210

10

Helix

213 – 215

3

Beta strand

216 – 218

3

Helix

224 – 240

17

Turn

241 – 243

3

Helix

248 – 256

9

Sequences

	Sequence		Length	Mass (Da)
	O28471 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 70CA739CA39A4863	FASTA	258	30,095
	10 20 30 40 50 60 MKDLKKIESY LDKLRIKEKD GEERKIYAEV LDGRTLKTLY KLSAKGYITA MGGVISTGKE 70 80 90 100 110 120 ANVFYADGVF DGKPVAMAVK IYRIETSEFD KMDEYLYGDE RFDMRRISPK EKVFIWTEKE 130 140 150 160 170 180 FRNLERAKEA GVSVPQPYTY MKNVLLMEFI GEDELPAPTL VELGRELKEL DVEGIFNDVV 190 200 210 220 230 240 ENVKRLYQEA ELVHADLSEY NIMYIDKVYF IDMGQAVTLR HPMAESYLER DVRNIIRFFS 250 KYGVKADFEE MLKEVKGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Structure and activity of the atypical serine kinase Rio1." Laronde-Leblanc N., Guszczynski T., Copeland T., Wlodawer A. FEBS J. 272:3698-3713(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 99-110, X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN PRESENCE AND ABSENCE OF ATP, PHOSPHORYLATION AT SER-108, MUTAGENESIS OF SER-108 AND ASP-196. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000782 Genomic DNA. Translation: AAB89445.1.

PIR

C69475.

RefSeq

NP_070631.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZP9	X-ray	2.00	A/B/C/D	1-258	[»]
1ZTF	X-ray	1.99	A	1-258	[»]
1ZTH	X-ray	1.89	A/B/C/D	1-258	[»]
3RE4	X-ray	2.00	A/B	1-258	[»]

ProteinModelPortal

O28471.

SMR

O28471. Positions 5-257.

ModBase

Search...

Protein-protein interaction databases

STRING

224325.AF1804.

PTM databases

PhosSite

P0507125.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB89445; AAB89445; AF_1804.

GeneID

1485027.

KEGG

afu:AF1804.

Phylogenomic databases

eggNOG

COG1718.

KO

K07178.

OMA

YIQGDPR.

ProtClustDB

CLSK2747046.

Enzyme and pathway databases

BioCyc

AFUL224325:GJBC-1839-MONOMER.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR018934. RIO-like_kinase.
IPR000687. RIO_kinase.
IPR018935. RIO_kinase_CS.
[Graphical view]

Pfam

PF01163. RIO1. 1 hit.
[Graphical view]

SMART

SM00090. RIO. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS01245. RIO1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O28471.

Entry information

Entry name

RIO1_ARCFU

Accession

Primary (citable) accession number: O28471

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program