KPC1_ASPNG
ID KPC1_ASPNG Reviewed; 1096 AA.
AC Q00078;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein kinase C-like;
DE EC=2.7.11.13;
GN Name=pkcA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; U10549; AAA97433.1; -; Genomic_DNA.
DR PIR; S61917; S61917.
DR AlphaFoldDB; Q00078; -.
DR SMR; Q00078; -.
DR STRING; 5061.CADANGAP00013618; -.
DR PRIDE; Q00078; -.
DR VEuPathDB; FungiDB:An18g02400; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1096957; -.
DR VEuPathDB; FungiDB:ATCC64974_109970; -.
DR VEuPathDB; FungiDB:M747DRAFT_92702; -.
DR VEuPathDB; FungiDB:M747DRAFT_92720; -.
DR VEuPathDB; FungiDB:M747DRAFT_92726; -.
DR eggNOG; KOG0694; Eukaryota.
DR BRENDA; 2.7.11.13; 518.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0005856; C:cytoskeleton; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0030427; C:site of polarized growth; IEA:EnsemblFungi.
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:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IEA:EnsemblFungi.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
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..1096
FT /note="Protein kinase C-like"
FT /id="PRO_0000055742"
FT DOMAIN 1..67
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 148..225
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 231..349
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 771..1030
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1031..1096
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 459..507
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 527..577
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 67..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 896
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 777..785
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 800
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1096 AA; 122235 MW; 859B2DB3B30D5BD8 CRC64;
MDGDDLIASV YRKIEREKAL ITAASNMRQS TDNPLVQQRV DANIRDGRKN IAYLEEKMRE
LQLRRMEHEG GGSPTDKRLP PNPEAGPVPP QKDYGPGYGG NEEYGDASGA YPHGGAGSMP
SGAPYADPRP FAPVPKARPN YTKLDLIKYD TQYLGPKIQL MLSQLEFKLS VEKQYKAGIE
KMVRLYQDEG DRKSRADAEG RRIESNQKIQ LLKQALKRYE DLHVDIESTD TPDDESLSTP
NLRKPLTGLL TLRIHAVKDV DHAASSRFSR GPETFIVLKV EDTIKARTKA TRIDRWQDET
FNIDIDKANE IELTVYDKSG DRPTPIGMLW VRISDIAEEM RRKKIESEFN ASGWVSADKM
EHGGAPGRPD TAGGAGSAHP SGPGGPGAAP SQGYGDGSAG APAGNQVMID SWFALEPVGR
IYLSMSFAKQ LKDRRPFDIG LNRQGAVRQK KEEVHEKQGH KFVTQQFYNI MRCALCGDFL
KYAAGMQCAD CKYTCHKKCY PKVVTKCISK ANYETDPDEE KINHRIPHRF EGFSNISANW
CCHCGYLLPF GRKNAKRCTE CGLTCHSHCT HLVPDFCGMS MEAANQILET LIRTKNHNKT
ASVSSGLSGR TLRPSGTPQG PQDSAAMAYP QKPVESPYGA PQRQPSAEAV SAATNSYMPP
QSPTAAARQQ MPPRTSSSAA VAAATVATGM PSPQQMPAEQ NRPMQPQLPT YDPKAYEPYA
NAPQGMPPQA IQHAAPAGYG MPAQQPAMQM VSQQPPEAPQ QPKVRIGLDH FNFLAVLGKG
NFGKVMLAET KSTKRLYAIK VLKKEFIIEN DEVESTKSEK RVFMIANKER HPFLLNLHAC
FQTETRVYFV MEYISGGDLM LHIQRGQFGL KRAQFYAAEV LLALKYFHEN GVIYRDLKLD
NIMLTLDGHI KVADYGLCKE NMWYGATTST FCGTPEFMAP EILLDKRYGR AVDWWAFGVL
IYQMLLQQSP FRGEDEDEIY DAILADEPLY PIHMPRDSVS ILQKLLTREP ELRLGSGPTD
AQEVMSHAFF RNINWDDIYH KRVPPPFLPQ ISSPTDTSNF DQEFTSVTPV LTPVQSVLSQ
AMQEEFRGFS YTADFA
