ID   Q18KA3_HALWD            Unreviewed;       305 AA.
AC   Q18KA3;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=rio2 {ECO:0000313|EMBL:CAJ51548.1};
GN   Synonyms=pkn1 {ECO:0000313|EMBL:CAJ51548.1};
GN   OrderedLocusNames=HQ_1420A {ECO:0000313|EMBL:CAJ51548.1};
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51548.1, ECO:0000313|Proteomes:UP000001975};
RN   [1] {ECO:0000313|EMBL:CAJ51548.1, ECO:0000313|Proteomes:UP000001975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA   Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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DR   EMBL; AM180088; CAJ51548.1; -; Genomic_DNA.
DR   RefSeq; WP_011570703.1; NC_008212.1.
DR   AlphaFoldDB; Q18KA3; -.
DR   STRING; 362976.HQ_1420A; -.
DR   GeneID; 4194473; -.
DR   KEGG; hwa:HQ_1420A; -.
DR   eggNOG; arCOG01181; Archaea.
DR   HOGENOM; CLU_018693_1_0_2; -.
DR   Proteomes; UP000001975; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05144; RIO2_C; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR030484; Rio2.
DR   InterPro; IPR015285; RIO2_wHTH_N.
DR   InterPro; IPR000687; RIO_kinase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR   PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR   Pfam; PF01163; RIO1; 1.
DR   Pfam; PF09202; Rio2_N; 1.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ51548.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001975};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:CAJ51548.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ51548.1}.
FT   DOMAIN          65..291
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
SQ   SEQUENCE   305 AA;  34763 MW;  1282C1238267EC73 CRC64;
     MVRNVAGVMT ELEPEDFYLL SGVEQGMRFS EWVNRGKLPQ LSGLSPEEVG YRLDRCATRE
     LIERKTIQYE GYTLKAEGYD ALALRTFSKR ETVDGVGAPL GVGKESDVLE VKSYKPLALK
     FHREGYTNFR EVMRERDYTA DNEHVSWLYT ARKAAEREYE VLEALYPDVS VPQPIDQNRH
     AIVMDKFESV ELNRAQLPQQ QAVGVLELIL REMQCAYENG YVHADMSEYN VAVSEDGVTV
     FDWPQAVSTD HENAHERLCR DISNLLTYFE RKYPNSTDRI DAESDAVRIA NSIAAGQFES
     VDAIP
//