ID Q8CJT6_STRCO Unreviewed; 632 AA. AC Q8CJT6; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 133. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:CAD55485.1}; GN OrderedLocusNames=SCO4481 {ECO:0000313|EMBL:CAD55485.1}; GN ORFNames=SCD65.24 {ECO:0000313|EMBL:CAD55485.1}, SCD69.01 GN {ECO:0000313|EMBL:CAD55485.1}; 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:CAD55485.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAD55485.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}. 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; AL939120; CAD55485.1; -; Genomic_DNA. DR RefSeq; NP_733639.1; NC_003888.3. DR RefSeq; WP_011029686.1; NZ_VNID01000017.1. DR AlphaFoldDB; Q8CJT6; -. DR STRING; 100226.gene:17762126; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR PaxDb; 100226-SCO4481; -. DR PATRIC; fig|100226.15.peg.4551; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_029615_0_0_11; -. DR InParanoid; Q8CJT6; -. DR OrthoDB; 4334148at2; -. 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; cd00161; RICIN; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.80.10.50; -; 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; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAD55485.1}; 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:CAD55485.1}; KW Transferase {ECO:0000313|EMBL:CAD55485.1}. FT DOMAIN 23..282 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 304..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 376..509 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..320 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 405..419 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 473..509 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 632 AA; 64103 MW; 356DB29C71598930 CRC64; MLELDGSGAE PLRDGDPRWI GPIPLIGRLG SGGMGRVYLG VHEGRYAAVK QLLPSVVAED EDFLRRFGHE LDNLARLPGE ATAPLLAGDR EARPPWFATA YVPGLTLTEA LEVHGGPLPA GALWLLLREA AKGLAAVHAL DMVHRDLKPS NVMLTLEGLT LIDFGVARAA EQSRLTRTGM VVGTPAYMSP EQASGRRASS GAVDVFALGS VLAYAASGRP PFGDESGHAV LYRIVHEEPD LGPLRELDPE LADVVASCLD KDHEGRPTAA ELLETAERHG PYEPPLWPEA LTERLTERAA FVTKLPERAD LPEPEPEPER DPGPGPGSAV LGRRDPGRSD HRRRHRVLFA VVPVVVAAGA TLAVQLLPYT FAPGDRADAS PSSSAPVSSA PAASPAGPGK ASRTATPDQD RSASPSRSPG EQGDRRGDAD GGGGAAGGSQ GDADAGGAGS GSGSGSGSAG DGGAGAGSGA GSGDGSGSDS GSGSGADSGS GAGSGSGSGS GSGSGDGGAS GSGVFTLKNA KNGRCLTTAH ADAPYDGDCT GDAATWTFRS RPDGTVWIIN GLLGRCIYTA AIGHPVFSFP CGRTTGQEWR VGSGGTLKNA ATGGCVTVSA MSGTGVRNEA CEQSAAQRWT RS //