ID KPC1_TRIRE STANDARD; PRT; 1139 AA. AC Q99014; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 04-APR-2006, entry version 48. DE Protein kinase C-like (EC 2.7.11.13). GN Name=pkc1; OS Trichoderma reesei (Hypocrea jecorina). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea. OX NCBI_TaxID=51453; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=QM9414 / Rut C-30; RX MEDLINE=96158841; PubMed=8569684; DOI=10.1007/s004380050047; RA Morawetz R., Lendenfeld T., Mischak H., Muehlbauer M., Gruber F., RA Goodnight J., de Graaff L.H., Visser J., Mushinski J.F., Kubicek C.P.; RT "Cloning and characterisation of genes (pkc1 and pkcA) encoding RT protein kinase C homologues from Trichoderma reesei and Aspergillus RT niger."; RL Mol. Gen. Genet. 250:17-28(1996). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Stimulated about twofold by phospholipids or CC phorbol esters. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. PKC CC subfamily. CC -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers. CC -!- SIMILARITY: Contains 2 REM (Hr1) repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U10016; AAA97432.1; -; Unassigned_DNA. DR PIR; S61918; S61918. DR HSSP; P31751; 1GZK. DR InterPro; IPR000008; C2. DR InterPro; IPR002219; DAG_PE_bd. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR011072; PKN_effector. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000861; REM_rpt_rho_bd. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF02185; HR1; 2. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR PRINTS; PR00008; DAGPEDOMAIN. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00742; Hr1; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 2. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. KW ATP-binding; Kinase; Metal-binding; Nucleotide-binding; KW Phorbol-ester binding; Repeat; Serine/threonine-protein kinase; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 1139 Protein kinase C-like. FT /FTId=PRO_0000055745. FT REPEAT 5 77 REM 1. FT REPEAT 154 229 REM 2. FT DOMAIN 814 1073 Protein kinase. FT ZN_FING 454 502 Phorbol-ester/DAG-type 1. FT ZN_FING 522 572 Phorbol-ester/DAG-type 2. FT NP_BIND 820 828 ATP (By similarity). FT COMPBIAS 667 678 Poly-Ala. FT COMPBIAS 733 739 Poly-Gln. FT COMPBIAS 762 768 Poly-Gln. FT ACT_SITE 939 939 Proton acceptor (By similarity). FT BINDING 843 843 ATP (By similarity). SQ SEQUENCE 1139 AA; 126055 MW; 937BB0DAB727B65C CRC64; MNEDEAIQNI TKKIEREKAL INAANAMRSQ TNNEAVRSPL DSQMRDGRRN LQFFEEKLRD IQLRKVGQGV EGMSLGADDA GRPPPPPKDA SSAAWGDQAA YGQQSQVGPP SDLAPPRHNF GAPGPGAASK ARPNFTKLDL IKYDTPYLGP RIQHMLSQIQ FKLNVEEQYL KGVEKMVQLY GMEGDRKSKA DAAARRVESK QKILLLKQAL KRYEELHVDM DSADAQDDDS INTPNLRKPL SGQLSIRVVA IKDVDHATTG RFARGPETFV AVKVEDTVMA RTKVSRNDRW EAEYHNMEVD KANEIELTIY DKPGEHPMPI AMLWVRISDI VEEMRRKRIE AEMNSSGWVS ADRMGSTGAP SQFPMSPTSG SFGGSPQAPG GGQGQAPGPF GDPAPQPQVV TGPIDGWFNL EPAGQIQLEF SFVKENRDKR QVDLGLGRKG AVRQRKEEVH EMFGHKFVQH QFYNIMPCAL CGDFLKYSAG MQCEDCKYTC HNKCYPSVVT KCISKSNAET DPDEEKINHR IPHRFQPFSN VTANWCCHCG YILPFGKKNC RKCSECGLTS HAQCVHLVPD FCGMSMAVAN QILEGIRVQK QRQQKTTSLS EKTLRSGATK SPTTAGHGSS ASFSSAGAGS VPGTPSAEAT EAARLMYNQT SPQRPGQPGR APSDLSAAAA ASAAMAAAQG RTGYDSGPQD PYGQGHYGAA GPAPQHHKYN PADYANVDQG FPAQPPAQQR PPQPQQQQQA PPAQMPPQQP PPQQPLPPQP GQQYQQQQPA AQKPQPQPPA TAQGAAAGPP GSQRKALPSA TDPGTGARIG LDHFNFLAVL GKGNFGKVML AETKRSKRLF AIKVLKKEFI IENDEVESIK SEKRVFLIAN RERHPFLTNL HACFQTETRV YFVMEYISGG DLMLHIQRGQ FGTKRAQFYA AEVCLALKYF HENGVIYRDL KLDNIMLTLD GHIKIADYGL CKEDMWYGST TSTFCGTPEF MAPEILLDKK YGRAVDWWAF GVLIYQMLLQ QSPFRGEDED EIYDAILADE PLYPIHMPRD SVSILQKLLT REPDQRLGSG PTDAQEVMSQ PFFRNINWDD IYHKRVQPPF LPQIKSATDT SNFDSEFTSV TPVLTPVQSV LSQAMQEEFR GFSYTADLD //