KPC1_HYPJE
ID KPC1_HYPJE Reviewed; 1139 AA.
AC Q99014;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein kinase C-like;
DE EC=2.7.11.13;
GN Name=pkc1;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX PubMed=8569684; DOI=10.1007/bf02191821;
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 protein
RT kinase C homologues from Trichoderma reesei and Aspergillus niger.";
RL Mol. Gen. Genet. 250:17-28(1996).
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=2.7.11.13;
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=2.7.11.13;
CC -!- ACTIVITY REGULATION: Stimulated about twofold by phospholipids or
CC phorbol esters.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; U10016; AAA97432.1; -; Unassigned_DNA.
DR PIR; S61918; S61918.
DR AlphaFoldDB; Q99014; -.
DR SMR; Q99014; -.
DR PRIDE; Q99014; -.
DR BRENDA; 2.7.11.13; 6451.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR CDD; cd08689; C2_fungal_Pkc1p; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037778; C2_fungal_PKC.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR037312; PKC-like_HR1.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF02185; HR1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 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 SUPFAM; SSF46585; SSF46585; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1139
FT /note="Protein kinase C-like"
FT /id="PRO_0000055745"
FT DOMAIN 1..67
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 142..219
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 225..343
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 814..1073
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1074..1139
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 454..502
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 522..572
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 72..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 939
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 820..828
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 843
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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
