ID   A0A0R3R351_9BILA        Unreviewed;       242 AA.
AC   A0A0R3R351;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Phorbol-ester/DAG-type domain-containing protein {ECO:0000313|WBParaSite:BTMF_0001444101-mRNA-1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001444101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0001444101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   ---------------------------------------------------------------------------
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   AlphaFoldDB; A0A0R3R351; -.
DR   STRING; 42155.A0A0R3R351; -.
DR   WBParaSite; BTMF_0001444101-mRNA-1; BTMF_0001444101-mRNA-1; BTMF_0001444101.
DR   Proteomes; UP000050602; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20833; C1_cPKC_rpt1; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   PANTHER; PTHR22968:SF27; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          93..143
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          158..208
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   242 AA;  27765 MW;  6141F22C840B64BD CRC64;
     LMYQKFEKPN SGANLDAHSD YNEDSRHDGA EHGGKSRMPS SCRRVGDALR KKSQAYLKFL
     STRKALRKLQ RIEGKGIVRK GALRQKNVHE VKAHKFIARF FKQPTFCSHC KEFLWGLNKQ
     GFQCQVCALV VHKRCHQFVN FQCPGADKGV DTDDPRQQHK WKVHSYSSPT FCDHCGSLLY
     GIIHQGKKCE CCDVNVHHKC VKYVPDMCGT DYIERRGRIH LSIRVDNDLL QVKGVISCSL
     FQ
//