PKCA_ASPFU
ID PKCA_ASPFU Reviewed; 1106 AA.
AC Q4WVG0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein kinase C {ECO:0000303|PubMed:26295576};
DE EC=2.7.11.13 {ECO:0000305|PubMed:26295576};
GN Name=pkcA {ECO:0000303|PubMed:26295576};
GN ORFNames=AFUA_5G11970 {ECO:0000312|EMBL:EAL91416.1};
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF GLY-579.
RX PubMed=26295576; DOI=10.1371/journal.pone.0135195;
RA Rocha M.C., Godoy K.F., de Castro P.A., Hori J.I., Bom V.L., Brown N.A.,
RA Cunha A.F., Goldman G.H., Malavazi I.;
RT "The Aspergillus fumigatus pkcA G579R mutant is Defective in the activation
RT of the cell wall integrity pathway but is dispensable for virulence in a
RT neutropenic mouse infection model.";
RL PLoS ONE 10:e0135195-e0135195(2015).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-579.
RX PubMed=27473315; DOI=10.1534/g3.116.031112;
RA Rocha M.C., Fabri J.H., Franco de Godoy K., Alves de Castro P., Hori J.I.,
RA Ferreira da Cunha A., Arentshorst M., Ram A.F., van den Hondel C.A.,
RA Goldman G.H., Malavazi I.;
RT "Aspergillus fumigatus MADS-Box transcription factor rlmA is required for
RT regulation of the cell wall integrity and virulence.";
RL G3 (Bethesda) 6:2983-3002(2016).
RN [4]
RP FUNCTION.
RX PubMed=32005734; DOI=10.1128/aem.02347-19;
RA Rocha M.C., Fabri J.H.T.M., Simoes I.T., Silva-Rocha R., Hagiwara D.,
RA da Cunha A.F., Goldman G.H., Canovas D., Malavazi I.;
RT "The cell wall integrity pathway contributes to the early stages of
RT Aspergillus fumigatus asexual development.";
RL Appl. Environ. Microbiol. 86:0-0(2020).
RN [5]
RP FUNCTION, INTERACTION WITH HSP90, AND MUTAGENESIS OF GLY-579.
RX PubMed=33010083; DOI=10.1111/cmi.13273;
RA Rocha M.C., Minari K., Fabri J.H.T.M., Kerkaert J.D., Gava L.M.,
RA da Cunha A.F., Cramer R.A., Borges J.C., Malavazi I.;
RT "Aspergillus fumigatus Hsp90 interacts with the main components of the cell
RT wall integrity pathway and cooperates in heat shock and cell wall stress
RT adaptation.";
RL Cell. Microbiol. 23:e13273-e13273(2021).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-579.
RX PubMed=33705521; DOI=10.1093/genetics/iyab036;
RA Rocha M.C., Fabri J.H.T.M., da Silva L.P., Angolini C.F.F., Bertolini M.C.,
RA da Cunha A.F., Valiante V., Goldman G.H., Fill T.P., Malavazi I.;
RT "Transcriptional control of the production of Aspergillus fumigatus
RT conidia-borne secondary metabolite fumiquinazoline C important for
RT phagocytosis protection.";
RL Genetics 0:0-0(2021).
CC -!- FUNCTION: Protein kinase C; part of cell wall integrity (CWI) signaling
CC pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the
CC downstream rlmA transcription regulator (PubMed:26295576,
CC PubMed:27473315). The CWI signaling pathway regulates cell wall
CC integrity and pyomelanin formation (PubMed:26295576). CWI controls also
CC oxidative stress response, gliotoxin production, iron adaptation and
CC asexual development (PubMed:26295576, PubMed:32005734). Finally, CWI is
CC constitutively required for A.fumigatus to cope with the temperature
CC increase found in the mammalian lung environment, during infection
CC (PubMed:33010083). Modulates the expression of fumiquinazoline cluster
CC during conidiogenesis (PubMed:33705521). {ECO:0000269|PubMed:26295576,
CC ECO:0000269|PubMed:27473315, ECO:0000269|PubMed:32005734,
CC ECO:0000269|PubMed:33010083, ECO:0000269|PubMed:33705521}.
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 -!- SUBUNIT: Interacts with hsp90. {ECO:0000269|PubMed:33010083}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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; AAHF01000003; EAL91416.1; -; Genomic_DNA.
DR RefSeq; XP_753454.1; XM_748361.1.
DR SMR; Q4WVG0; -.
DR STRING; 746128.CADAFUBP00005826; -.
DR EnsemblFungi; EAL91416; EAL91416; AFUA_5G11970.
DR GeneID; 3511583; -.
DR KEGG; afm:AFUA_5G11970; -.
DR VEuPathDB; FungiDB:Afu5g11970; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_54_0_1; -.
DR InParanoid; Q4WVG0; -.
DR OMA; NRIYFAM; -.
DR OrthoDB; 222529at2759; -.
DR PHI-base; PHI:5065; -.
DR Proteomes; UP000002530; Chromosome 5.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0031505; P:fungal-type cell wall organization; IDA:AspGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
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 Gene3D; 2.60.40.150; -; 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; PF00168; C2; 1.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Virulence; Zinc; Zinc-finger.
FT CHAIN 1..1106
FT /note="Protein kinase C"
FT /id="PRO_0000453183"
FT DOMAIN 1..67
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 149..226
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 232..350
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 781..1040
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1041..1106
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 460..508
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 528..578
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 65..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 906
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 787..795
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 810
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1082
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MOD_RES 1101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MUTAGEN 579
FT /note="G->R: Blocks the ativation of the cell wall
FT integrity pathway, abolishes the interaction with hsp90,
FT and impairs the production of fumiquinazoline C."
FT /evidence="ECO:0000269|PubMed:26295576,
FT ECO:0000269|PubMed:33010083, ECO:0000269|PubMed:33705521"
SQ SEQUENCE 1106 AA; 123066 MW; 62E4A7510A79704D CRC64;
MDGDDLIASV YRKIEREKAL ITAASNMRQS TDNPLVQQRV DANIRDGRKN IAYLEEKMRE
LQLRQMKQEG ASPTDKRLPP NPDGSAPVPP PKDYAPGYSG HEREYGDASG AYPHGGAGTM
PSGAPFADPR PFAPVPKARP NYTKLDLIKY DTPYLGPKIQ LMLSQLEFKL SVEKQYKAGI
EKMVRLYQDE GDRKSRQDAE GRRIESNQKI QLLKQALKRY EDLHVDIESA EAPDDESLST
PNLRKPLTGL LTLRIHAVED VDHAASSRFS RGPETFVVVK VEDAIKARTK ATRTDKWQDE
PFNIEIDKAN EIELTVYDKS GDRPTPIGML WVRISDIAEE MRRKKIESEF NASGWVSADK
MEHGAAHGRQ DAGGAPGSSN RPPSGGHSGG PGQGYAGGAP GGASAGPVLI DSWFALEPVG
RIHLTLSFAK QLKDRRPFDI GLNRQGAVRQ KKEEVHEKQG HKFVTQQFYN IMRCALCGDF
LKYAAGMQCA DCKYTCHRKC YPKVVTKCIS KANYETDPDE EKINHRIPHR FEGFSNISAN
WCCHCGYLLP FGRKSAKRCT ECGLTCHAQC THLVPDFCGM SMEAANQILE TLIRAKNHNK
SASVSSGLSG RTLRPGGPPQ APQDNVALAY PQKPVEGAYG APQRQPSAEA ISAATNTYIP
PQSPTAAQRQ HIPPRTSSSQ SPAAAAAAAA AAATGLRTPQ QASDPNRPVQ PPPSSHAHYD
PAAYASYQQA IPPQAMQKMG APYGMPQQQQ QQAVAPMQQQ VAVKEEIPPQ QPKVRIGLDH
FNFLAVLGKG NFGKVMLAET KSTKKLYAIK VLKKEFIIEN DEVESTKSEK RVFLIANKER
HPFLLNLHAC FQTETRVYFV MEYISGGDLM LHIQRGQFGL KRAQFYAAEV LLALKYFHEN
GVIYRDLKLD NILLTLDGHI KIADYGLCKE NMWYGSTTST FCGTPEFMAP EILLDKKYGR
AVDWWAFGVL IYQMLLQQSP FRGEDEDEIY DAILADEPLY PIHMPRDSVS ILQKLLTREP
ELRLGSGPTD AQEVMSHAFF RNINWDDIYH KRVPPPFLPT ISSPTDTSNF DQEFTSVTPV
LTPVQSVLSQ AMQEEFRGFS YTADFA
