ID   Q18EX2_HALWD            Unreviewed;       349 AA.
AC   Q18EX2;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=rio1 {ECO:0000313|EMBL:CAJ53495.1};
GN   Synonyms=pkn2 {ECO:0000313|EMBL:CAJ53495.1};
GN   OrderedLocusNames=HQ_3398A {ECO:0000313|EMBL:CAJ53495.1};
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ53495.1, ECO:0000313|Proteomes:UP000001975};
RN   [1] {ECO:0000313|EMBL:CAJ53495.1, 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   -!- 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; CAJ53495.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q18EX2; -.
DR   STRING; 362976.HQ_3398A; -.
DR   KEGG; hwa:HQ_3398A; -.
DR   eggNOG; arCOG01180; Archaea.
DR   HOGENOM; CLU_018693_3_3_2; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; 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; cd05145; RIO1_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   InterPro; IPR008266; Tyr_kinase_AS.
DR   NCBIfam; NF041310; Prot_Kin_Rio1_Halo; 1.
DR   PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR   PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR   Pfam; PF01163; RIO1; 1.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS01245; RIO1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ53495.1};
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:CAJ53495.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ53495.1}.
FT   DOMAIN          125..349
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  38967 MW;  6BDE58AD79579C28 CRC64;
     MTDHDHDNNH ENSGHRSDID NAEDEAEAEA DIESTDAEMS KINAETTDSD SGFVAPDVVD
     TPGNEWAEID VSDTEADRIA RRRDREFSTF RERLTDADQF KVEQSVFDDA TFAAIYKLVQ
     DDHIAAFGGP ISTGKEANVY EARGTDTADV AVKIYRINAS NFQQMRSYLE GDPRFDGLGQ
     DKKAIVLAWT QKEFANLRRA MRAGVRVPEP IAVERNVLVM ELVGLVEERA RRLAEVDIEN
     PQTAYEVVQE YMQRLYSAGL IHGDLSEYNM IIHNGELVVI DLGQAVTVHH PNAEMFLRRD
     CKNVATFFSR QGIDTDPAAL IETVTEPDPD PSGTLAQSEH SVQSTDEES
//