ID A0A0D2GM82_9EURO Unreviewed; 1162 AA.
AC A0A0D2GM82;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN ORFNames=Z517_05055 {ECO:0000313|EMBL:KIW82028.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW82028.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW82028.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW82028.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000946};
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; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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; KN846971; KIW82028.1; -; Genomic_DNA.
DR RefSeq; XP_013285836.1; XM_013430382.1.
DR AlphaFoldDB; A0A0D2GM82; -.
DR STRING; 1442368.A0A0D2GM82; -.
DR GeneID; 25304545; -.
DR VEuPathDB; FungiDB:Z517_05055; -.
DR HOGENOM; CLU_000288_54_0_1; -.
DR OrthoDB; 21591at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20822; C1_ScPKC1-like_rpt1; 1.
DR CDD; cd20823; C1_ScPKC1-like_rpt2; 1.
DR CDD; cd08689; C2_fungal_Pkc1p; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR CDD; cd05570; STKc_PKC; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24351:SF228; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF46585; HR1 repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KIW82028.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..68
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 168..245
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 251..369
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 476..524
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 544..594
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 837..1096
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1097..1162
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 63..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1162 AA; 130337 MW; 294686376EFCCB0C CRC64;
MADPDQAIAE VYRKIEREKA LINAATHMRQ STNNAAVQAR VDSNIRDSRR NISYLEEKLA
ELQLRQRGHN EGVAPPPPAH GGSGYQTPSD SRMQQSRFQH GGGPTPPPKD ERGYFSNERG
DYGDPGPGGY SQGGTGMMPP RAPYGDPRPY NAPVPKARPN FSKLDLIKYD TPYLGPKIQL
MLSQLEFKLS VEKQYKAGIE KMVRLYQDEG DRKSRLDAEG RRIESNQKVQ LLKQALKRYM
DLHVDIETSD AADDDSLNAP NMRKPLTGHL EMRIHAIKDV DHAASSRFSR GPETFVIMKV
EDNIRAKTRA TRTDKWTEET HHVDIDKANE IELTVYDKAG DRPTPIGFLW IRISDIAEEM
RRKKIESEFQ QNGWVSADKM ANGGSPGKPG PDFQSTPFMP PGDAAGAGSA AGFAQNSQQQ
FQPVMIDSWF SLEPAGRIHL SMSFQKQTGG KRPFDIGLNR QGAVRQKKEE VHEKQGHKFV
KQQFYNVMRC ALCGDFLKYS AGMQCADCKY TCHTKCYPKV VTKCISKANY ETDPDEEKIN
HRIPHRFDNF SNIGANWCCH CGYLLPLGRR NAKKCSECGL TCHAQCQHLV PDFCGMSMIV
ANEILETIQR TKHHNKSSSV SSGMSNRTLR PNSAARPGPT SPTQSFISDS TTLTPQISNQ
SYDQHQEQPK PSAAAMSAAQ NMMYNQPQAS QSQPFQQQQQ QRPLQQKAVS TAAVQAAAAA
TNRPPSQQYN QSFNDYSPQK VPADRYANAR PPAPEQPHAS YDPRAYQGYV QPAQQQAPQH
QAPQQAIIQS QRPQPQAAAA AASYAPAPIK PAPSSQQQVA TPPSGRGSGP RIGLDHFNFL
AVLGKGNFGK VMLAEAKSSK KLYAIKVLKK EFIIENDEVE STKSEKRVFL IANKERHPFL
LNLHACFQTE TRVYFVMEYI SGGDLMLHIQ RGQFGLKRAQ FYAAEVCLAL KYFHENGVIY
RDLKLDNILL TLDGHIKIAD YGLCKEDMWY GSTTSTFCGT PEFMAPEILL DKKYGRAVDW
WAFGVLIYQM LLQQSPFRGE DEDEIYDAIL ADEPLYPIHM PRDSVSILQK LLTREPELRL
GSGPGDAEEI MNHAFFKGIN WDDIYHKRVP TPFKPTIKNE KDTSNFDQEF TSVTPVLTPV
QSVLSPAHQE EFRGFSYTAD FI
//
