ID   A0A0N5CEI7_STREA        Unreviewed;       813 AA.
AC   A0A0N5CEI7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Protein kinase C {ECO:0000313|WBParaSite:SPAL_0001627500.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001627500.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001627500.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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DR   AlphaFoldDB; A0A0N5CEI7; -.
DR   STRING; 174720.A0A0N5CEI7; -.
DR   WBParaSite; SPAL_0001627500.1; SPAL_0001627500.1; SPAL_0001627500.
DR   Proteomes; UP000046392; Unplaced.
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   CDD; cd20798; C1_CeDKF1-like_rpt2; 1.
DR   CDD; cd01239; PH_PKD; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR   PANTHER; PTHR22968:SF15; SERINE_THREONINE-PROTEIN KINASE DKF-1; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          155..205
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          246..296
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          506..766
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   813 AA;  91908 MW;  7F28C73891898666 CRC64;
     MISNWMQNLT NSNNSGITNN NSIGNNTNTF NVQPLGNQNV CQVNSVMDFV SSINVNDKQT
     ITITMQFGNI KETLTLVRNC DSESFENLKK KARILAESAL HDNNVNVTNS SDLYLFVHNY
     NAPNMLQHLS SLDQLDNGSV VEVVRIERNE KPTRPHSLNV NSYKTPTFCD YCGEILVGLI
     RQGLQCSLCK CNFHKKCAFA SRNNCAKNDK KPSSSQKFSI GADGFIQPPI LSEDQSLTPS
     QAFELPHTLA VHNYKTPTIC RVCDKMLLGL IKQGLKCRDC KVNVHKKCAG LLPMNCKISE
     NAITPNMDNA SINEQTFHNV LNLSTNMEGL DEHMEDQDSL IPLARLPGQA AVRTQKRGPV
     IESWMVHFLL SDPERRLKHY WVLTDGVISL YNEYNGGVNP YRVYKQIQLS EILLLQPYDG
     PPVHPKFPPH CFEIRTIHNQ VICVGEYLPV DISNQKKYST TSNINQAICV VQNWYHTLQQ
     ALQPPQLKSD PVSAEPALQF AQLYQVQSDK ILGSGQFGTV FSGVHRLSGR EVAIKVIAKD
     RFSKKNSSTI DTLKTEVAIL QNISYHGIIR LESMFETKDK IFVVMEKMNG DMLEMILSQE
     MGRLNERITK FLIIQILLAL RYLHLKNICH ADMKPENVLV SDITIAFPQT KLCDFGYARF
     IGDAQFRKTI VGTPAYLAPE VLQKKGYNKK LDMWSLSVII YVTLSGTFPF NDGEEINDQI
     QNAAFMFPTD PWKEISNEAI DLIQKLFKVE IDARLSIEET LAHPWLQDPQ ILADIRDLET
     RLGIRYMSTE LEQIISPSFT PIIPSRVINT SLI
//