ID Q0SDK0_RHOJR Unreviewed; 534 AA. AC Q0SDK0; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 120. 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_ro02581 {ECO:0000313|EMBL:ABG94386.1}; OS Rhodococcus jostii (strain RHA1). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94386.1, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000431; ABG94386.1; -; Genomic_DNA. DR RefSeq; WP_011595293.1; NC_008268.1. DR AlphaFoldDB; Q0SDK0; -. DR KEGG; rha:RHA1_ro02581; -. DR PATRIC; fig|101510.16.peg.2612; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR OrthoDB; 5169909at2; -. 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:0106310; F:protein serine kinase activity; IEA:RHEA. 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; 1. 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:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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:ABG94386.1}; 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:ABG94386.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339..362 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 14..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 277..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 382..431 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..327 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 401..419 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 534 AA; 56027 MW; 500F27E7F51DB6E0 CRC64; MAAGSRVGTQ FGQYQLRALL GRGGMGEVYE AFDTVKGRTV AVKLLDLELA NDATFQQRFR RESHVAARLQ EPHVIPIHDW GEIDGVLYID MRLVPGQDLR SLLRSQGPMD ASRAVVIMEQ IASALDAAHA DGLVHRDVKP ENILVTANDF AYLVDFGIAH SSSDLRLTTL GSAVGSYAYM APERFDNAPV DGRADVYSLA CVLHECLTGA IPFPSNSISS AIRAHLAAPA PRPSAVRPDI PAAFDGVVAT GLAKSRDARY RTAGALAAAA RAALSGRPPA RTEVAGLHAP TRIDSVGRPP EYPSTSVPQG PLAPPPHHPP PRSSYAAGPP PQKRRSTAVP VMVTLLVVAV LALGGVVGWL VLDRNRSDDP LTAAVTTIAQ PPVVRTSTES AAPAPPPTIP SATTRTTTTR TTTTRTTVAA PPLVGEVSGT DGQGFMSPAD ARCNHTNPAA FIGRTTKSLV VVCQTGVGRY YYQGVRISDG AAISVDDPVP NGSGFVATNA GNGTQYRVTP TALTIVGGDG QVIATEPMVE SAYR //