ID   RIO1_THEAC              Reviewed;         186 AA.
AC   Q03021;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=RIO-type serine/threonine-protein kinase Rio1;
DE            EC=2.7.11.1;
DE            EC=3.6.3.-;
GN   Name=rio1; OrderedLocusNames=Ta0396;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=1408839; DOI=10.1093/nar/20.19.5226;
RA   Klenk H.-P., Renner O., Schwass V., Zillig W.;
RT   "Nucleotide sequence of the genes encoding the subunits H, B, A' and A'' of
RT   the DNA-dependent RNA polymerase and the initiator tRNA from Thermoplasma
RT   acidophilum.";
RL   Nucleic Acids Res. 20:5226-5226(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- FUNCTION: Despite the protein kinase domain is proposed to act
CC       predominantly as an ATPase (By similarity).
CC       {ECO:0000250|UniProtKB:G0S3J5}.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000305}.
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DR   EMBL; X68198; CAA48285.1; -; Genomic_DNA.
DR   EMBL; AL445064; CAC11539.1; -; Genomic_DNA.
DR   PIR; S26727; S26727.
DR   AlphaFoldDB; Q03021; -.
DR   SMR; Q03021; -.
DR   STRING; 273075.Ta0396m; -.
DR   EnsemblBacteria; CAC11539; CAC11539; CAC11539.
DR   KEGG; tac:Ta0396; -.
DR   eggNOG; arCOG01180; Archaea.
DR   HOGENOM; CLU_018693_3_3_2; -.
DR   OMA; PYGFYRN; -.
DR   Proteomes; UP000001024; 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; IPR000687; RIO_kinase.
DR   InterPro; IPR018935; RIO_kinase_CS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01245; RIO1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..186
FT                   /note="RIO-type serine/threonine-protein kinase Rio1"
FT                   /id="PRO_0000213536"
FT   ACT_SITE        124
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   ACT_SITE        140
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
SQ   SEQUENCE   186 AA;  21739 MW;  64E2FC7F0AF6C18A CRC64;
     MVFRAVSGKK FVAVKIFKMS TLKFMSIRKY IEGDQRFSKI RIDRNDIVPV WVRKEYTNLM
     ALENAHVPAP KPIGFFKNIL VMSYIGTKSG PAPQLKDVEI DEGIYDQVID GMRRMYANRI
     VHADLSEYNM LFHRKVYFID LAQAVDMDHP MAAEFLERDI VNVSNFFQKH GIETDPDKIR
     EYIKKK