ID   Q0SAP1_RHOJR            Unreviewed;       731 AA.
AC   Q0SAP1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=RHA1_ro03592 {ECO:0000313|EMBL:ABG95395.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG95395.1, 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; ABG95395.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SAP1; -.
DR   KEGG; rha:RHA1_ro03592; -.
DR   PATRIC; fig|101510.16.peg.3620; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031634; PknG_rubred.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16919; PknG_rubred; 1.
DR   Pfam; PF16918; PknG_TPR; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABG95395.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABG95395.1}.
FT   DOMAIN          108..369
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   731 AA;  81041 MW;  5EE1F41F06A743B2 CRC64;
     MSDETRRTPM DDPQSTRGVR FDPFADDDDD DVPSARTVPD AAHTSDLSML LTNPVLAEHK
     RYCDRCKRPV GRSTAARPGD TEGVCTHCGT VFSFAPQLEA GELVAGQYEV LGCLAHGGVG
     WIYLALDHNV SDRWVVLKGL LHSGDPEAQE VALAERRFLA EVTHPSIVKI YNFVEHPGMD
     GNPIGYIVME YVRGRTLRDL LTELKEDAGP DDPKPMLPVE HAIRYLLEVT PALGYLHSMG
     LVYNDLKPEN IMIGDDYDQL KLIDMGAVAR IGDHGYIYGT QGYQAPEIAT TGPTVASDIY
     TVGRTLAVVT LDMPTAGGCY VDGLPTPEEA PLLAEYEFYH RLLLRAIHPD PARRFASAEE
     MSTQLEGVLR EVRAQQTGHP QPGLSHRFSP QRTTFGTDLT ISRTDVYVDG HRRDERISAM
     SIVRALPIPL VDPDDPAAPL LSVVHSRPRE LLDSLHRAKE VADDGVASTS IEIPLAEVRA
     HLDLGQPRDA ATILESLDHQ REDTWRVDWH TGLCALVGGD FEAAFTRFDS VLTALPGEEA
     PKLALAATAE MWCEYRSGED IGRWRRTAEK YYCTVWRTDH GAVSAAFGLS RQLEHRDDRA
     AAVEALDEVP PTSRHYAEAR LTSVLMLVHD RPLAEVSERD LQEAARRVEL LAHDERRALQ
     TRVLVLGVAV DWLHAGGIPE TTRILSVPFT ERGLRTGAES ALRALARKAP ERRHRYTLVD
     LANLIRPTTW L
//