ID   A0A0R3S2X8_9BILA        Unreviewed;       112 AA.
AC   A0A0R3S2X8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Nucleocapsid protein {ECO:0000313|WBParaSite:EEL_0000909501-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000909501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000909501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent
CC       protein kinase activity, this protein interacts with the catalytic
CC       subunit of the enzyme after the cAMP-induced dissociation of its
CC       regulatory chains. {ECO:0000256|ARBA:ARBA00002844}.
CC   -!- SIMILARITY: Belongs to the PKI family. {ECO:0000256|ARBA:ARBA00006393}.
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DR   AlphaFoldDB; A0A0R3S2X8; -.
DR   WBParaSite; EEL_0000909501-mRNA-1; EEL_0000909501-mRNA-1; EEL_0000909501.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:InterPro.
DR   InterPro; IPR004171; cAMP_dep_PKI.
DR   Pfam; PF02827; PKI; 1.
PE   3: Inferred from homology;
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   112 AA;  12237 MW;  B0474171F1D384FA CRC64;
     MDDATQAKDS TAEDDQMKSF VNSGRSGRRN AIPEVDARGV DPDATKLAER LSLMNTDGQD
     NYTVDDTTGN GIEIGLKLKV SKLSSFRCFA TWCFLEEVNL FNLSAPTSHS SL
//