ID A0A386WKM0_9ACTN Unreviewed; 424 AA. AC A0A386WKM0; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 24-JAN-2024, entry version 13. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AYF28936.1}; GN ORFNames=CSH63_16030 {ECO:0000313|EMBL:AYF28936.1}; OS Micromonospora tulbaghiae. OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Micromonospora. OX NCBI_TaxID=479978 {ECO:0000313|EMBL:AYF28936.1, ECO:0000313|Proteomes:UP000267804}; RN [1] {ECO:0000313|EMBL:AYF28936.1, ECO:0000313|Proteomes:UP000267804} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNY-010 {ECO:0000313|EMBL:AYF28936.1, RC ECO:0000313|Proteomes:UP000267804}; RA Kim M.C., Machado H., Jensen P.R., Fenical W.; RT "Integration of genomic and chemical information greatly accelerates RT assignment of the full stereostructure of myelolactone, a potent inhibitor RT of myeloma from a marine-derived Micromonospora."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; 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; CP024087; AYF28936.1; -; Genomic_DNA. DR AlphaFoldDB; A0A386WKM0; -. DR KEGG; mtua:CSH63_16030; -. DR Proteomes; UP000267804; Chromosome. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR011045; N2O_reductase_N. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR47197:SF3; DIHYDRO-HEME D1 DEHYDROGENASE; 1. DR PANTHER; PTHR47197; PROTEIN NIRF; 1. DR SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:AYF28936.1}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AYF28936.1}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000313|EMBL:AYF28936.1}. FT SIGNAL 1..40 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 41..424 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5017200038" SQ SEQUENCE 424 AA; 45644 MW; 197DED617CE60641 CRC64; MTPVPPRPSR SRRRAGLAVL AALALVAPAP LVTAPAPATA AVALQEVMFV GNNWDGTADI IRSRGDYARL GRINVIPDRA ARLREIYLNP IKLAFFLGIR QGPGEGHDQL IDDMYTTPDG TALVVSRPSF ADVVSIDLAT GALRWRFPVS GYRADHMAVS PDGTRVAVSA STSNTVHVLD IRTGAQLGSF GAGDKPHENI YTDGGTRLWN MSIGEVNTDL DAPWLDWTKG DRRITVADTG TYQVVKVIDM RDRLDAAGRR DLSDAVRPAV FTPDGSRLYF QVSFFNGVVE YDVATDRVTR VATLPKNPAT SEDRTTWVND SRHHGLSMSP DGTRICVAGT MDDYATVMDR ATLREGPLVS ASKPYWATVS GDGRDCVISE SGADQVTAIS FATGQKVASV PVGDHPQRVR IGHIPEGWTP PAAG //