RIO1_ARCFU
ID RIO1_ARCFU Reviewed; 258 AA.
AC O28471;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=RIO-type serine/threonine-protein kinase Rio1;
DE Short=AfRio1;
DE EC=2.7.11.1;
GN Name=rio1; OrderedLocusNames=AF_1804;
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 PROTEIN SEQUENCE OF 99-110, X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN
RP COMPLEX WITH ADP; ATP AND MANGANESE IONS, FUNCTION, PHOSPHORYLATION AT
RP SER-108, AND MUTAGENESIS OF SER-108 AND ASP-196.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=16008568; DOI=10.1111/j.1742-4658.2005.04796.x;
RA Laronde-Leblanc N., Guszczynski T., Copeland T., Wlodawer A.;
RT "Structure and activity of the atypical serine kinase Rio1.";
RL FEBS J. 272:3698-3713(2005).
CC -!- FUNCTION: Autophosphorylation of the rio1 protein is not necessary for
CC maintenance of kinase activity. Prefers ATP over GTP (PubMed:16008568).
CC The yeast ortholog is involved in ribosome biogenesis. Despite the
CC protein kinase domain is proposed to act predominantly as an ATPase (By
CC similarity). {ECO:0000250|UniProtKB:G0S3J5,
CC ECO:0000269|PubMed:16008568}.
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 Evidence={ECO:0000305|PubMed:16008568};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; AE000782; AAB89445.1; -; Genomic_DNA.
DR PIR; C69475; C69475.
DR RefSeq; WP_010879299.1; NC_000917.1.
DR PDB; 1ZP9; X-ray; 2.00 A; A/B/C/D=1-258.
DR PDB; 1ZTF; X-ray; 1.99 A; A=1-258.
DR PDB; 1ZTH; X-ray; 1.89 A; A/B/C/D=1-258.
DR PDB; 3RE4; X-ray; 2.00 A; A/B=1-258.
DR PDB; 4JIN; X-ray; 2.10 A; A=1-258.
DR PDBsum; 1ZP9; -.
DR PDBsum; 1ZTF; -.
DR PDBsum; 1ZTH; -.
DR PDBsum; 3RE4; -.
DR PDBsum; 4JIN; -.
DR AlphaFoldDB; O28471; -.
DR SMR; O28471; -.
DR STRING; 224325.AF_1804; -.
DR iPTMnet; O28471; -.
DR EnsemblBacteria; AAB89445; AAB89445; AF_1804.
DR GeneID; 24795547; -.
DR KEGG; afu:AF_1804; -.
DR eggNOG; arCOG01180; Archaea.
DR HOGENOM; CLU_018693_3_3_2; -.
DR OMA; EIRCAKV; -.
DR OrthoDB; 44076at2157; -.
DR PhylomeDB; O28471; -.
DR BRENDA; 2.7.11.1; 414.
DR EvolutionaryTrace; O28471; -.
DR PRO; PR:O28471; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Hydrolase; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..258
FT /note="RIO-type serine/threonine-protein kinase Rio1"
FT /id="PRO_0000344796"
FT DOMAIN 49..258
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 212
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:16008568, ECO:0007744|PDB:1ZP9"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16008568,
FT ECO:0007744|PDB:1ZP9"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16008568,
FT ECO:0007744|PDB:1ZP9"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O30245"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16008568,
FT ECO:0007744|PDB:1ZP9"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:16008568"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16008568,
FT ECO:0007744|PDB:1ZP9"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:16008568"
FT MOD_RES 108
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16008568"
FT MUTAGEN 108
FT /note="S->A: Absence of autophosphorylation, retains kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:16008568"
FT MUTAGEN 196
FT /note="D->A: Drastically reduced kinase activity."
FT /evidence="ECO:0000269|PubMed:16008568"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3RE4"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:1ZTH"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:1ZTH"
FT STRAND 59..70
FT /evidence="ECO:0007829|PDB:1ZTH"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1ZTH"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1ZTF"
FT HELIX 110..129
FT /evidence="ECO:0007829|PDB:1ZTH"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1ZTH"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:1ZTH"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1ZTF"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1ZTF"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1ZTF"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:1ZTH"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1ZTH"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:1ZTH"
SQ SEQUENCE 258 AA; 30095 MW; 70CA739CA39A4863 CRC64;
MKDLKKIESY LDKLRIKEKD GEERKIYAEV LDGRTLKTLY KLSAKGYITA MGGVISTGKE
ANVFYADGVF DGKPVAMAVK IYRIETSEFD KMDEYLYGDE RFDMRRISPK EKVFIWTEKE
FRNLERAKEA GVSVPQPYTY MKNVLLMEFI GEDELPAPTL VELGRELKEL DVEGIFNDVV
ENVKRLYQEA ELVHADLSEY NIMYIDKVYF IDMGQAVTLR HPMAESYLER DVRNIIRFFS
KYGVKADFEE MLKEVKGE
