RIO2_ARCFU
ID RIO2_ARCFU Reviewed; 282 AA.
AC O30245;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RIO-type serine/threonine-protein kinase Rio2;
DE Short=AfRio2;
DE EC=2.7.11.1;
GN Name=rio2; OrderedLocusNames=AF_2426;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH
RP ATP AND ATP ANALOG, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=15341724; DOI=10.1016/j.str.2004.06.016;
RA LaRonde-LeBlanc N., Wlodawer A.;
RT "Crystal structure of A. fulgidus Rio2 defines a new family of serine
RT protein kinases.";
RL Structure 12:1585-1594(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH MN-ATP AND MN-ADP,
RP AND PHOSPHORYLATION AT SER-128.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=15943813; DOI=10.1111/j.1742-4658.2005.04702.x;
RA LaRonde-LeBlanc N., Guszczynski T., Copeland T., Wlodawer A.;
RT "Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures
RT of its nucleotide-metal ion complexes.";
RL FEBS J. 272:2800-2810(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Mg(2+). Mn(2+) is seen in the crystal structure; there are 2
CC Mn(2+) ions in the ATP-bound crystal and 1 Mn(2+) in the ADP-bound
CC crystal.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15341724}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15943813}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91236.1; -; Genomic_DNA.
DR PIR; C69553; C69553.
DR RefSeq; WP_010879913.1; NC_000917.1.
DR PDB; 1TQI; X-ray; 2.00 A; A=1-282.
DR PDB; 1TQM; X-ray; 1.99 A; A=1-282.
DR PDB; 1TQP; X-ray; 2.10 A; A=1-282.
DR PDB; 1ZAO; X-ray; 1.84 A; A=1-282.
DR PDB; 1ZAR; X-ray; 1.75 A; A=1-282.
DR PDBsum; 1TQI; -.
DR PDBsum; 1TQM; -.
DR PDBsum; 1TQP; -.
DR PDBsum; 1ZAO; -.
DR PDBsum; 1ZAR; -.
DR AlphaFoldDB; O30245; -.
DR SMR; O30245; -.
DR STRING; 224325.AF_2426; -.
DR iPTMnet; O30245; -.
DR EnsemblBacteria; AAB91236; AAB91236; AF_2426.
DR GeneID; 24796150; -.
DR KEGG; afu:AF_2426; -.
DR eggNOG; arCOG01181; Archaea.
DR HOGENOM; CLU_018693_1_0_2; -.
DR OMA; GYTNFRE; -.
DR OrthoDB; 74143at2157; -.
DR PhylomeDB; O30245; -.
DR BRENDA; 2.7.11.1; 414.
DR EvolutionaryTrace; O30245; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..282
FT /note="RIO-type serine/threonine-protein kinase Rio2"
FT /id="PRO_0000347334"
FT DOMAIN 92..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:15943813"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15341724"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15943813,
FT ECO:0007744|PDB:1ZAO"
FT BINDING 180..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15341724,
FT ECO:0000269|PubMed:15943813, ECO:0007744|PDB:1TQP,
FT ECO:0007744|PDB:1ZAO"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15341724,
FT ECO:0007744|PDB:1TQP"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15943813,
FT ECO:0007744|PDB:1ZAR"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:15943813"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15341724,
FT ECO:0000269|PubMed:15943813, ECO:0007744|PDB:1TQP,
FT ECO:0007744|PDB:1ZAO"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:15943813"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:15943813"
FT MOD_RES 128
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15943813"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1ZAR"
FT TURN 23..27
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:1ZAR"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:1ZAR"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1ZAR"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 247..266
FT /evidence="ECO:0007829|PDB:1ZAR"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:1ZAR"
SQ SEQUENCE 282 AA; 32809 MW; 7DE69AF0EF8DB24D CRC64;
MNIAELYGKM GKHSWRIMDA IFKNLWDYEY VPLQLISSHA RIGEEKARNI LKYLSDLRVV
QNRQKDYEGS TFTFIGLSLY SLHRLVRSGK VDAIGKLMGE GKESAVFNCY SEKFGECVVK
FHKVGHTSFK KVKEKRDYGD LHFSVLAIRS ARNEFRALQK LQGLAVPKVY AWEGNAVLME
LIDAKELYRV RVENPDEVLD MILEEVAKFY HRGIVHGDLS QYNVLVSEEG IWIIDFPQSV
EVGEEGWREI LERDVRNIIT YFSRTYRTEK DINSAIDRIL QE
