ID Q9RDS3_STRCO Unreviewed; 686 AA. AC Q9RDS3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 151. DE SubName: Full=Probable serine/threonine protein kinase {ECO:0000313|EMBL:CAB66178.1}; GN OrderedLocusNames=SCO2244 {ECO:0000313|EMBL:CAB66178.1}; GN ORFNames=SC1G2.06c {ECO:0000313|EMBL:CAB66178.1}; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB66178.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAB66178.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H., RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). 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; AL939111; CAB66178.1; -; Genomic_DNA. DR RefSeq; NP_626493.1; NC_003888.3. DR AlphaFoldDB; Q9RDS3; -. DR STRING; 100226.gene:17759841; -. DR PaxDb; 100226-SCO2244; -. DR PATRIC; fig|100226.15.peg.2282; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2319; Bacteria. DR HOGENOM; CLU_000288_135_1_11; -. DR InParanoid; Q9RDS3; -. DR OrthoDB; 951193at2; -. DR PhylomeDB; Q9RDS3; -. DR Proteomes; UP000001973; Chromosome. 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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR45333:SF1; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-LIKE PROTEIN; 1. DR PANTHER; PTHR45333; MEMBRANE PROTEIN-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00400; WD40; 3. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAB66178.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAB66178.1}; KW Transferase {ECO:0000313|EMBL:CAB66178.1}; KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}. FT DOMAIN 15..279 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 364..395 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 546..580 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REGION 271..310 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..686 FT /note="Disordered" 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 686 AA; 71625 MW; 7FC39B662D441216 CRC64; MSRSASGIPA EIGPYRLERL LGEGGMGRVY LGRTPAGSAV AVKVVHRAYA ADPEFRRRFA LEVAAARRVQ GLYTVPVVAA DLDADEPWLA TAYAPGPSLQ QAVGERGPLP AAEVLALTAG VAEALETIHA AGVIHRDLKP SNIVLTADGP KVIDFGIARA ADVTALTATG MRAGTPAYMA PEYIRGQEVT EAGDVFALGL VAHFAATGRL AFGGGSDHGV AYRILEASPD LDGCPESVRG VVALCLEKDP ARRPTPAEIV RLCGRAANGD FDDGRTPTVV STPPATGPDA PTATAPARTP APDADPETPS TPPYAALLGV VAAIALVVVL VVTLLPSSGK PPKSKQPYPV VAATAIFARG TSGVAFSPDG ETLATGGQDG KVRLWDAATR KVRATLVEKG WYGPSRVVGV TFSADGKTLV TRTGTHLVGV WDVARRREVR RIEESAYSLA LSPDGKWIAL GDSAGANLWD LGRRGEDPRA HLSQNLHATD LAFSPDGRTL ASVGDFSDQR YQVENEPAKL WDLTRLDPRP YGQGDPRHNL ALEDVVYAVA FSPDGKTLAT GGQGGGVRLW DAATGRPKAT LTHKFVTEAR DLAFSPDGST LAVTAEGRVL LWNLADRKPS AILADDETGF GADINELAFS PDGRFLAGTT TGGGAPEETA APGTTEADAA KDSGVRLWKV PTKTAH //