ID   Q5JHS7_THEKO            Unreviewed;       311 AA.
AC   Q5JHS7;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=TK2250 {ECO:0000313|EMBL:BAD86439.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD86439.1, ECO:0000313|Proteomes:UP000000536};
RN   [1] {ECO:0000313|EMBL:BAD86439.1, ECO:0000313|Proteomes:UP000000536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC   {ECO:0000313|Proteomes:UP000000536};
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(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         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; AP006878; BAD86439.1; -; Genomic_DNA.
DR   RefSeq; WP_011251200.1; NC_006624.1.
DR   AlphaFoldDB; Q5JHS7; -.
DR   STRING; 69014.TK2250; -.
DR   EnsemblBacteria; BAD86439; BAD86439; TK2250.
DR   GeneID; 78448793; -.
DR   KEGG; tko:TK2250; -.
DR   PATRIC; fig|69014.16.peg.2205; -.
DR   eggNOG; arCOG01181; Archaea.
DR   HOGENOM; CLU_018693_1_0_2; -.
DR   InParanoid; Q5JHS7; -.
DR   OrthoDB; 50101at2157; -.
DR   PhylomeDB; Q5JHS7; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
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; IPR000719; Prot_kinase_dom.
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.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAD86439.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000536};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:BAD86439.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          98..311
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   311 AA;  35688 MW;  A9DCFFA8F25363CF CRC64;
     MVSKLLALEA YPSLRDLDFR ILRGVELNMR HHRWVPLEDI ARFARVDVET ASFRLGKLDD
     WGLVVRRSDI GYIGYQLTIH GYDALAIRAL AKKGVIEAIS TTQIGVGKDA DVYVGITPSG
     EKVAVKFNRI GGRTASRRAG YHGHVFQDKH HTSWLYVSRL IAKKEHEALV LLSPIARVPR
     PVAWNRHVVV MEFVEGTELA ELRDTDLTRE EAERILDRVL EEYLKIVRFG IVHSDMSEFN
     IVLTKDGDIL IIDWAQYIST AHPESYELLK RDITVLLNAF RRRWGVKKEF EKVWPEFESA
     WKESRGEEGG N
//