ID A0A226D8L4_FOLCA Unreviewed; 251 AA.
AC A0A226D8L4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phorbol-ester/DAG-type domain-containing protein {ECO:0000259|PROSITE:PS50081};
GN ORFNames=Fcan01_23536 {ECO:0000313|EMBL:OXA41892.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA41892.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA41892.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA41892.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA41892.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-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 -!- 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:OXA41892.1}.
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DR EMBL; LNIX01000028; OXA41892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226D8L4; -.
DR STRING; 158441.A0A226D8L4; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20834; C1_nPKC_theta-like_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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 142..192
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 214..251
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 21..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 28398 MW; 14D192B679DFFEB6 CRC64;
MDHYLHDCIE PYKLDAKMWT TPQNNHHHRG HPHHRAPPTP KSPHKIINYS SSPISNNKLL
NVHLFVQQAH GRPTRGVNSS SSSSASTCTT RTNSASTSLG MRLLSEGEGS IEEESSKESG
DAYNITGRRG AIKHQKVHEV KGHRFVAKFF RQPTFCAFCH DFLWGFGKQG YQCQLCQTSV
HKKCHVKLLG KCPGSGKESQ STIYLRERFK IDVPHRFKVN NFRSCTFCDH CGSLLYGLFK
QGLKCEGQHL H
//
