ID   Q0RXP9_RHOJR            Unreviewed;      1156 AA.
AC   Q0RXP9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Serine/threonine-protein kinase PknK {ECO:0000256|PIRNR:PIRNR000574};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000574};
DE   AltName: Full=Protein kinase K {ECO:0000256|PIRNR:PIRNR000574};
GN   OrderedLocusNames=RHA1_ro08893 {ECO:0000313|EMBL:ABG99937.1};
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL1 {ECO:0000313|EMBL:ABG99937.1,
OG   ECO:0000313|Proteomes:UP000008710}.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG99937.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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         ECO:0000256|PIRNR:PIRNR000574};
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         ECO:0000256|PIRNR:PIRNR000574};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|PIRNR:PIRNR000574}.
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DR   EMBL; CP000432; ABG99937.1; -; Genomic_DNA.
DR   RefSeq; WP_011599616.1; NC_008269.1.
DR   AlphaFoldDB; Q0RXP9; -.
DR   KEGG; rha:RHA1_ro08893; -.
DR   PATRIC; fig|101510.16.peg.8209; -.
DR   HOGENOM; CLU_006325_2_0_11; -.
DR   OrthoDB; 136365at2; -.
DR   Proteomes; UP000008710; Plasmid pRHL1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016236; Ser/Thr_kinase_PknK_prd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000574; Ser/Thr_PK_PknK_prd; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000574};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000574, ECO:0000313|EMBL:ABG99937.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000574};
KW   Plasmid {ECO:0000313|EMBL:ABG99937.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000574};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000574, ECO:0000313|EMBL:ABG99937.1}.
FT   DOMAIN          26..291
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          327..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  126945 MW;  A498902F333472AC CRC64;
     MPDDDTESTQ RQVDADVVAE LAAEGFEDAC IAGRGGFGIV YRCRQPALDR VVAVKVLSPD
     PDHMDRARFL REQQAMGRLS GHPNIVHVLQ AGITYTGRPY IVMPFHRRDS LDSWITKHGA
     LRAAEALAVG VKLAGALETA HRAGVLHRDI KPGNILLTEY GEPQLTDFGI ARITGGEETT
     RGLVAGSPAY TAPELLSGSD ASVVTDVYGL GATLFTALAG RPAFARRRGE QVFAQLLRIG
     TEPLPDLRDI GVPEAVCTVI ESAMARDPAE RPATAADLGG ALRRAGEHIG LALGDIPLPI
     VDEEDRPFRP SDEVEVGVSE YLRYRRGSGT RLDRPPPPSA STKYRPPVTP GVTVARTQLL
     ERLRRSGRPR LVLIHAPAGF GKSTLAAQRL AALRGEGVAT AWLTIDNDDN TLIWFLTHLI
     ESIAVAQPAF GRELVRELEV HGADRERYVL TSLIDQLHSS DHHVALVIDD WHRVSNEDTR
     SALAFLLEHG CHHLHLIVTS RTRLGLPLSR MSVRNELIEI DSSALRFDVR ESTQLLIDRS
     GLHLDAPDIV ELEQSTDGWA AALQLVSLAL RDHPHPRELI EHLSGGNRAI GEYLAENVLG
     NLDRSTLDFL LATSITEKIC GSLARALTDN REGQATLEDI ESRDLFLRRL DEEGRWFRYH
     HLFAEFLQHR LERDDPDRIV ELHRRAGRWF ADRHLLSQAV DHYILAGEQD DAVTLVEDAA
     MELLEQSQMG TLLGLAAKLP AKGTTDRPRL HIALAWAHAI LHHPRDAEQN LSAAETALDN
     AVDDRAAADM RAEATFILAP INVFDDKIDG LDEAVEGCMA RADTLRPWVM CGAADVASFR
     AIYRFDFDEA RRWQTWALPF HQRSTGPFSV LYGYCMAGIA AREQLDLPAA EASFRHAMAL
     AEADDGLGYG ARLTAALLGD LLYEQGHLAD ADHLLDRSHT LGAEGGTVDF LLATYGTGAR
     LKRLLGQNDA AKARLDEGAR LAQQLRLPRL AARVTNERVR TGIGHAAPGA PVIDRESRQL
     PARNNGIAVV TFELEEDSAI RAALTARDQD LEPVYERAHA LVESIERRVR PRAFLNAALL
     QVEVSATMGQ QDAALTELLP LAEQCARLGL IRPVLDAGPA VNRLARHLRT HLHERADAAA
     SIVLNQYLAD LEKQTI
//