ID A0A109UXE6_9SACH Unreviewed; 1135 AA.
AC A0A109UXE6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN ORFNames=AW171_hschr53177 {ECO:0000313|EMBL:AMD21242.1};
OS Eremothecium sinecaudum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD21242.1, ECO:0000313|Proteomes:UP000243052};
RN [1] {ECO:0000313|EMBL:AMD21242.1, ECO:0000313|Proteomes:UP000243052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD21242.1,
RC ECO:0000313|Proteomes:UP000243052};
RA Dietrich F.S.;
RT "Genome sequence of the yeast Holleya sinecauda.";
RL Submitted (JAN-2016) 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}.
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DR EMBL; CP014245; AMD21242.1; -; Genomic_DNA.
DR RefSeq; XP_017988238.1; XM_018132481.1.
DR AlphaFoldDB; A0A109UXE6; -.
DR STRING; 45286.A0A109UXE6; -.
DR GeneID; 28724520; -.
DR OrthoDB; 21591at2759; -.
DR Proteomes; UP000243052; Chromosome v.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
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; 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; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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 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..66
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 97..174
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 400..447
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 467..517
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 808..1067
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1068..1135
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 536..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 837
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1135 AA; 128849 MW; E098644D7099B7BC CRC64;
MLSNVEQDIL RKIEVERNII QGASALKKKT DNAQVIQKCN TSIRESQQNI QYLEDTLGRL
QMSETRQHAS STAHPGYGQL TTISPNEHRF SRLELAKFDC PSICQRNQYM LQLLEFKLSI
ERQYQAANDK LTKLYQIDGD QRSSSAAQGG AYKSKQRIQL LTKALKKYQA INVDIDGYRD
HGDDSSNGQH KFRRKQLTGD LTIGISSISD VDHIQSPLFS KKPETVITIK VDDVMKGSTK
PSKTDRWHDE FHIHVEKGNE VEITVYDRIN DRVVPVAVLW LLLSDIAEEI RKKKIGQTGS
AWYDVGDVLP DSDPYGDTSA AHLAIDALNY RTRVKSSAET TNDHSTPVTS NAWFVLEPAG
QILLTLGFNK STQDQRKDLK GLRRHGAIVN RKDDIYEKHG HHFVQKSFYN IMCCAYCGDF
LRYTGFQCQD CKFLCHKKCY GNIVTKCIAK TSTEVDPDET KLNHRIPHRF EPTSNRGTKW
CCHCGYILPW GKKSVRKCTE CSVMCHAQCA HLVPDFCGMS MEMAAKVLTT IKNTNLGHQQ
KRTSSPTPIQ VSEPQGDDYD EFPERIESKT SESVPEKSAY MQVVNPDPLN RHAYDSHVVQ
DMPQVKDQES PTIALNSDEK MHDTIEKQVD YNNAADEAYL KFTNASISQK NSANDLRSTL
DPGPPVSSNY NADVREYAAY VRDKVIRDED FASTEDNRSE ISRQHQLPEP IDPAMLNLKQ
NPFNVECMTE EPTSLIATNE FDNLAASLDA KAATALEAFE ASQGIVEKPA QDTRISPVQT
TPQQRVRPAS NRQKRKTPKR RKVTLDDFVL LKVLGKGNFG KVLLARSKNT DRLCAIKVLK
KDHIIQNHDI ESARAEKKVF LLATKAKHPF LTNLYCSFQT ENRIYFAMEF VGGGDLMWHV
QNKRLSVRRA KFYAAEVLLA LKYFHDNGII YRDLKLENIL LTLEGHIKIA DYGLCKDNMW
DGHRTATFCG TPEFMAPEIL KEEAYTKAVD WWAFGVLLYQ MLLCQSPFSG DDEDEVFNAI
LTDEPLYPID MAGDIVQIFQ GLLTKDPEKR LGRGVRDALE VMEEPFFSNI NFDDVYHLRV
EPPYIPKLKA ADDTSYFEKE FTTAPPNLTP LPSILSASLQ EEFRGFSFMP DDLVL
//
