ID   Q0S1U4_RHOJR            Unreviewed;       737 AA.
AC   Q0S1U4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 118.
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_ro06720 {ECO:0000313|EMBL:ABG98492.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG98492.1, 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; ABG98492.1; -; Genomic_DNA.
DR   RefSeq; WP_011598535.1; NC_008268.1.
DR   AlphaFoldDB; Q0S1U4; -.
DR   KEGG; rha:RHA1_ro06720; -.
DR   PATRIC; fig|101510.16.peg.6780; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_012667_0_0_11; -.
DR   OrthoDB; 4569664at2; -.
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; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:ABG98492.1};
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   Transferase {ECO:0000313|EMBL:ABG98492.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        492..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        586..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        615..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        673..693
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        705..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          158..464
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   737 AA;  81607 MW;  C9DA177A8B7081AF CRC64;
     MYERTDLVES AERTRTALAT VVARFSEAWG SGSPPDLSAF LPREPAERRS ILIELIKIDL
     EYRWVRHCFP KRLTEYRAEF AELQEGPLPA DLVYEEFHAL RRSAHGVDTA TMAAEAATMA
     GGPDLDELTS DYCSTMIARP LAQVVLGNID VGDRVDDFDL LMRIGSGAFA QVYLARQQSM
     QRLVAVKISH NHGIEPQTLA QLDHEYIVRI FDQRLIADGE LKLLYMQYLP GGTLLDVVHL
     LRSTPPEHRS GQLLLDAVDG VLAAKGEVRP SESAVRARAS ALTWPETVAW LGCRLADALQ
     HASERGVLHR DIKPANVLLS AEGIPKLADF NVSASNRIKG TSPLAYFGGS LAYMSPEQLE
     ACHPGSPATA ADLDTRSDIF ALAVMLWELL TGRRPFADET SAGESETSLA RMLELRRSPV
     EAKFLSELPP DCPMALRRVL LKCLSPDRDD RYPSGSELAQ QLDLCLEERS RDLVYPPPNS
     WRARLSRSPT PILWSSSLVG IGLATIYLAV HLQELLNERL SDATYAKLYT STIVFNLCAW
     PLAVLIYAYM SRDLLAVPRG LRKGRRYDEA VLARVRSRTL VWGDMCALNT FVFAVCASVA
     GVMFLRWFTD LPARLMVHAA TTVLVAGTIS VAYTFFLSTF YVVRCVYPIY LRHGLTTAHD
     TVVLRGLRRR TTVYLAVTAS VPLVGVLAGF STLEPAELPL VRDSVLGLCA ASGLAFVAVY
     WLYRKLDADV RALERVV
//