O30245 (RIO2_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RIO-type serine/threonine-protein kinase Rio2
Short name=AfRio2
EC=2.7.11.1

Gene names

Name:	rio2
Ordered Locus Names:	AF_2426

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	282 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium. Mangenese is seen in the crystal structure; there are 2 Mn2+ ions in the ATP-bound crystal and 1 Mn2+ in the ADP-bound crystal.
Subunit structure	Monomer. Ref.2
Post-translational modification	Autophosphorylated. Ref.3
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 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 protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 282

282

RIO-type serine/threonine-protein kinase Rio2

PRO_0000347334

Regions

Domain

94 – 236

143

Protein kinase

Nucleotide binding

99 – 104

6

ATP

Nucleotide binding

180 – 186

7

ATP

Nucleotide binding

222 – 223

2

ATP

Sites

Active site

218

1

Proton acceptor By similarity

Metal binding

103

1

Magnesium 1

Metal binding

223

1

Magnesium 2

Metal binding

235

1

Magnesium 1

Metal binding

235

1

Magnesium 2

Binding site

120

1

ATP

Binding site

126

1

ATP

Binding site

235

1

ATP

Amino acid modifications

Modified residue

128

1

Phosphoserine; by autocatalysis Ref.3

Secondary structure

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282

Helix Strand Turn

Details...

Helix

3 – 8

6

Helix

12 – 22

11

Turn

23 – 27

5

Beta strand

29 – 32

4

Helix

33 – 40

8

Helix

44 – 56

13

Beta strand

59 – 63

5

Beta strand

65 – 67

3

Beta strand

69 – 72

4

Helix

74 – 87

14

Beta strand

92 – 100

9

Beta strand

102 – 111

10

Turn

112 – 114

3

Beta strand

115 – 122

8

Helix

143 – 160

18

Turn

161 – 163

3

Beta strand

164 – 166

3

Beta strand

169 – 173

5

Beta strand

176 – 180

5

Helix

187 – 189

3

Helix

195 – 211

17

Beta strand

223 – 227

5

Beta strand

230 – 233

4

Helix

247 – 266

20

Helix

272 – 280

9

Sequences

	Sequence		Length	Mass (Da)
	O30245 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7DE69AF0EF8DB24D	FASTA	282	32,809
	10 20 30 40 50 60 MNIAELYGKM GKHSWRIMDA IFKNLWDYEY VPLQLISSHA RIGEEKARNI LKYLSDLRVV 70 80 90 100 110 120 QNRQKDYEGS TFTFIGLSLY SLHRLVRSGK VDAIGKLMGE GKESAVFNCY SEKFGECVVK 130 140 150 160 170 180 FHKVGHTSFK KVKEKRDYGD LHFSVLAIRS ARNEFRALQK LQGLAVPKVY AWEGNAVLME 190 200 210 220 230 240 LIDAKELYRV RVENPDEVLD MILEEVAKFY HRGIVHGDLS QYNVLVSEEG IWIIDFPQSV 250 260 270 280 EVGEEGWREI LERDVRNIIT YFSRTYRTEK DINSAIDRIL QE

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]	"Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases." LaRonde-LeBlanc N., Wlodawer A. Structure 12:1585-1594(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH ATP AND ATP ANALOG, FUNCTION, MASS SPECTROMETRY, SUBUNIT. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[3]	"Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes." LaRonde-LeBlanc N., Guszczynski T., Copeland T., Wlodawer A. FEBS J. 272:2800-2810(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEXES WITH MN-ATP AND MN-ADP, PHOSPHORYLATION AT SER-128. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000782 Genomic DNA. Translation: AAB91236.1.

PIR

C69553.

RefSeq

NP_071248.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TQI	X-ray	2.00	A	1-282	[»]
1TQM	X-ray	1.99	A	1-282	[»]
1TQP	X-ray	2.10	A	1-282	[»]
1ZAO	X-ray	1.84	A	1-282	[»]
1ZAR	X-ray	1.75	A	1-282	[»]

ProteinModelPortal

O30245.

SMR

O30245. Positions 1-282.

ModBase

Search...

Protein-protein interaction databases

STRING

224325.AF2426.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB91236; AAB91236; AF_2426.

GeneID

1485657.

KEGG

afu:AF2426.

Phylogenomic databases

eggNOG

COG0478.

KO

K07179.

OMA

KYHRIGR.

ProtClustDB

CLSK2747315.

Enzyme and pathway databases

BioCyc

AFUL224325:GJBC-2478-MONOMER.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR018934. RIO-like_kinase.
IPR015285. RIO2_kinase_winged_hlx_N.
IPR000687. RIO_kinase.
IPR008266. Tyr_kinase_AS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF01163. RIO1. 1 hit.
PF09202. Rio2_N. 1 hit.
[Graphical view]

SMART

SM00090. RIO. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50011. PROTEIN_KINASE_DOM. False negative.
PS01245. RIO1. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O30245.

Entry information

Entry name

RIO2_ARCFU

Accession

Primary (citable) accession number: O30245

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program