ID   A0A016SMA4_9BILA        Unreviewed;       168 AA.
AC   A0A016SMA4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Phorbol-ester/DAG-type domain-containing protein {ECO:0000259|PROSITE:PS50081};
GN   Name=Acey_s0205.g1917 {ECO:0000313|EMBL:EYB91486.1};
GN   ORFNames=Y032_0205g1917 {ECO:0000313|EMBL:EYB91486.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB91486.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYB91486.1}.
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DR   EMBL; JARK01001541; EYB91486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SMA4; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.20; -; 1.
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; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          95..145
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          40..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  18578 MW;  F7BB87A5ACB074E5 CRC64;
     MMHFPGPGFI IEITEGEDVE AHVSDGITNI FMGQQAKKNV EATASKTQRA EIEPHGSDAE
     GSHQGKERVL KERNDPSNDK QRSSGTPGKI HEVSGHKFMA VLLPQPSFCA HCKEFIYGIG
     KQGYQCQGCS MVVHKRCHEQ VVWKCSGNKA DNIEEAKQEV YTCSSLFV
//