ID A0A364KMI9_9EURO Unreviewed; 764 AA. AC A0A364KMI9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 24-JUL-2024, entry version 21. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN ORFNames=BHQ10_000778 {ECO:0000313|EMBL:RAO64766.1}; OS Talaromyces amestolkiae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces; OC Talaromyces sect. Talaromyces. OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO64766.1, ECO:0000313|Proteomes:UP000249363}; RN [1] {ECO:0000313|EMBL:RAO64766.1, ECO:0000313|Proteomes:UP000249363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIB {ECO:0000313|EMBL:RAO64766.1, RC ECO:0000313|Proteomes:UP000249363}; RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7; RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L., RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.; RT "Differential ?-glucosidase expression as a function of carbon source RT availability in Talaromyces amestolkiae: a genomic and proteomic RT approach."; RL Biotechnol. Biofuels 10:161-161(2017). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. {ECO:0000256|ARBA:ARBA00023596}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RAO64766.1}. 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; MIKG01000001; RAO64766.1; -; Genomic_DNA. DR AlphaFoldDB; A0A364KMI9; -. DR STRING; 1196081.A0A364KMI9; -. DR OrthoDB; 232702at2759; -. DR Proteomes; UP000249363; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro. DR CDD; cd14135; STKc_PRP4; 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 InterPro; IPR050494; Ser_Thr_dual-spec_kinase. DR InterPro; IPR044092; STKc_PRP4. DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1. DR PANTHER; PTHR24058:SF103; MITOGEN-ACTIVATED PROTEIN KINASE-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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000249363}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 439..761 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..239 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 266..407 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..56 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 63..80 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..153 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..177 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 205..223 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..345 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 468 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 764 AA; 87038 MW; 01CE2836B5F48F83 CRC64; MASRRSRSLS TPSEGEIVES GSETKATTSQ TSMNDTNVNR RSRLSPSFSP RSPASGAARS PPSRRRSRSR SRTRSPYRRG GKRRRYDDYD DYDNYRHGSS SSYRYESRSE HDRRYDSRRQ RTYHDYDRDD SYNGGLRYMD DYDRRDKRQK TRSRSPFRDV RKPKKYDDAD DIGEPRKVAF RNQSVSERGV SPVVAQDVKP HTEPGRQVES STEVSTGLNG SSPDLTEAPE EILDEAARLE ARRKRREAIK AKYRGQDALR IQALHQGADP DLTPVTPMSA AESPKSPALE VSTETPESEF TVAKDEDLAN GTQPMEGVEK DEPSAADYDP TQDMREERQR HDQQFSEDVS SAAYDETKTT KQDVLIPEPQ PEAPAKDPYD MFAEDDDDMF APEPEEQPEH ASAKAVPKAK ELDMTMLDNW DDPEGYYNVR LGELINGRYH VHQNLGKGMF SSVVRATDSK TDKYVAIKII RNNDTMRKAG MKEIQILEQL LEADPDDKKH VIRFERYFDH KGHLCMVFEN LSMNLREVLK KFGRDVGLNL RAIRAYAQQM FLGLSLLRKC NILHADLKPD NLLVNEQRSV LKICDLGSAS SASDNDITPY LVSRFYRAPE IILGVPYDYA IDIWSIGCTL YELYTGKILF TGRNNNQMLR SIMECRGKFP PKFLRKGALT GAHFDDMLNF HSTEEDKLTG RVVTKVLDFK KPTRDLKSRL MGTGSGGKGS KGMTESETKE LAQFVDLLDR CLSVNPEKRC TPVEALKHPF ISRK //