ID Q9L0I0_STRCO Unreviewed; 599 AA. AC Q9L0I0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 141. DE SubName: Full=Protein serine/threonine kinase {ECO:0000313|EMBL:CAB82016.1}; GN Name=pkaD {ECO:0000313|EMBL:CAB82016.1}; GN OrderedLocusNames=SCO4777 {ECO:0000313|EMBL:CAB82016.1}; GN ORFNames=SCD63.09 {ECO:0000313|EMBL:CAB82016.1}; 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:CAB82016.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAB82016.1, 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; AL939121; CAB82016.1; -; Genomic_DNA. DR RefSeq; NP_628935.1; NC_003888.3. DR AlphaFoldDB; Q9L0I0; -. DR STRING; 100226.gene:17762426; -. DR PaxDb; 100226-SCO4777; -. DR PATRIC; fig|100226.15.peg.4850; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_63_44_11; -. DR InParanoid; Q9L0I0; -. DR OrthoDB; 9762169at2; -. DR PhylomeDB; Q9L0I0; -. DR Proteomes; UP000001973; 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; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.40.1000.10; Mog1/PsbP, alpha/beta/alpha sandwich; 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; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 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:CAB82016.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Transferase {ECO:0000313|EMBL:CAB82016.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381..399 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 13..268 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 286..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 403..447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 411..435 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 599 AA; 63938 MW; BDF9EB783C54B0F9 CRC64; MNQMQGRLVA GRYRLGEAIG SGGMGRVWRA HDEVLHRTVA IKELTAALYV SESDQAILLA RTRGEARAAA RINHSAVVTV HDVLEHDGRP WIVMELVEGR SLADAVKEEE RVDPREAARV GLWVLRALRA AHTAGVLHRD VKPGNVLLAD DGRVLLTDFG IAQIEGDSTI TRTGEVVGSV DYLAPERVRG HDPGPSSDLW ALGATLYTAV EGRSPFRRTS PLTTMQAVVE EEATEPRYAG ALAPVISALL RKDPAERPDA TEAEHLLAQA AEGRRPDAAQ AYVPTTRYEG PPRAGDTAVQ GMPAGGSGAT PYPQAGGSGA TPYPPTTGPT GAGPAPTGHT RGGYTQVGHT EGGYTAPGYA PAPAVGGAAP GRARRVRMRT LALVVAVAAL IGAGTAVVLH QRDEGGSSAG ADPTQGPTGS AAPSPSPSAS ATTGKGPGGS VPADWTRRDD PLGFSLYLPE NWQRRDFDGD SGELRQIDYT PDGGNHVLRI SVDTAPDYND PYAHQQDLDA QLLQRLVDYR RVKLERAGYR DRDSARWEYT WTALAKDTEF PGPRRAVSQM YMSRDGVEYA LNMTGPAGDW PTTQRRFKAV LQGWQEETG //