ID   Q0SJE5_RHOJR            Unreviewed;       619 AA.
AC   Q0SJE5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
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=RHA1_ro00505 {ECO:0000313|EMBL:ABG92341.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92341.1, 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   -!- 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};
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DR   EMBL; CP000431; ABG92341.1; -; Genomic_DNA.
DR   RefSeq; WP_011593767.1; NC_008268.1.
DR   AlphaFoldDB; Q0SJE5; -.
DR   KEGG; rha:RHA1_ro00505; -.
DR   PATRIC; fig|101510.16.peg.533; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3391; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 4455641at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14952; NHL_PKND_like; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR035016; NHL_PKND.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF01436; NHL; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51125; NHL; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABG92341.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:ABG92341.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          370..411
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          417..453
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          454..495
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          506..537
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          288..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   619 AA;  64767 MW;  3244F1B059D7308E CRC64;
     MGGAELEPGD VFAGYTIQRV LGVGGMGAVY LARDPHLPRN TALKLLDRSL TTDDCFRSRF
     ELEADHAARL EHPNIVSVFD RGREANQHWI AMQYVAGTDA AVALREGPMD PPRAVHIVAE
     TAKALDYAHE NGVLHRDVKP ANILLGMSGA GQPERVLLTD FGIAKALDET QHLTRTGSLV
     ATLQYSAPEA FQGIPLDLRA DVYSLGCTLF CLLTGHPPFT GSTQEVMRGH LCGPVPRISA
     VRGDLPPTFD DIVSAALTKR REDRLPSCHA LSAGVQLALS RMQSAQTAKQ ILTRRQTANV
     HAAPDTPTSR QPTPRRQGQQ LPPLAPQPPP PQRNSVPPRR KRAGVLLALA LLALLAVGAA
     VVFVSWPNRS ATQTTLPFEG LDYPVGVAVN TAGDLVVADS NNNRVLRLAA GAGAQEVLPF
     TDLDHPSGVA TNGAGDVFVA DTRNNRVLEL AAGATTQTVL PFTGLAGPAG VAVSDAGHLF
     VADNNNNRIV ALPAGAASPQ VLPLSDLHGP VGVAVNSGGD VFVTDTDNNR VLFLPAGATD
     QTVLPFTGLA SPTGVAADST GVFVADYGGG RVVALRAGAD TPAVVRFTGL HGPIWVAVTA
     TGDLVVTDGD RVLQLSGDG
//