ID Q9RYI0_DEIRA Unreviewed; 524 AA. AC Q9RYI0; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 153. 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=DR_A0332 {ECO:0000313|EMBL:AAF12449.1}; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF12449.1, ECO:0000313|Proteomes:UP000002524}; RN [1] {ECO:0000313|EMBL:AAF12449.1, ECO:0000313|Proteomes:UP000002524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524}; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans RT R1."; RL Science 286:1571-1577(1999). 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; AE001825; AAF12449.1; -; Genomic_DNA. DR PIR; A75588; A75588. DR RefSeq; NP_285655.1; NC_001264.1. DR RefSeq; WP_010889591.1; NZ_JMLF01000011.1. DR AlphaFoldDB; Q9RYI0; -. DR STRING; 243230.DR_A0332; -. DR PaxDb; 243230-DR_A0332; -. DR EnsemblBacteria; AAF12449; AAF12449; DR_A0332. DR GeneID; 69519216; -. DR KEGG; dra:DR_A0332; -. DR PATRIC; fig|243230.17.peg.3224; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_519464_0_0_0; -. DR InParanoid; Q9RYI0; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000002524; Chromosome II. 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; IBA:GO_Central. 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:AAF12449.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002524}; KW Transferase {ECO:0000313|EMBL:AAF12449.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 422..441 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 453..474 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 503..521 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 50..314 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 325..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 330..351 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..378 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..410 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 79 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 524 AA; 55298 MW; 79807356E6BE2AED CRC64; MTAPQTCPFC GSPAAPTDTV CHVCGAALGR GGATALLTLP PGTTLQGGQY VLDRVLGQGG FGITYDARDT RLGMRVAVKE LFVDGSTRRG LNVIPPLSQG AEVFAATRRG FLEEAQVLAR FGDPSIVRVL NYFEENGTAY LVMEFLEGET LGEAIQKRGP LPPLIAAQVA DSVAHALEVV HAAGLLHRDI KPDNIFLHHS GRIILIDFGS VRAFDSGKTV AHTRLVTPGY APLEQYSSAA KFGPYTDLYA LGATLFHALT GQMPPAATDL SLGTPLPPLP PGTPPNLREA VLSCMAPRIE NRPQSAQALR RILRGEGTVT VTAAPAAAPA PQPQSQPVRP SPAPTPTPMP NPQTDREVEK RLRELEKEVR KEARRQSRRP APAPAPIPIP APAPQRPAPP PTPFPGPRRP AAPRDGTLGR RLVVVAITVL SALSGGILMA QTPAWQIISP PELSVMAGAG IGALAGLALG QLLWWALPVA LPIFAAAITS SVCQNLGYRP PTVIAASVAA IVVSLILMRL IRRI //