ID R0KNY1_NOSB1 Unreviewed; 146 AA.
AC R0KNY1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Protein kinase C zeta type {ECO:0000313|EMBL:EOB12381.1};
GN Name=KPCZ {ECO:0000313|EMBL:EOB12381.1};
GN ORFNames=NBO_453g0004 {ECO:0000313|EMBL:EOB12381.1};
OS Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS (Pebrine of silkworm).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB12381.1, ECO:0000313|Proteomes:UP000016927};
RN [1] {ECO:0000313|EMBL:EOB12381.1, ECO:0000313|Proteomes:UP000016927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT "Comparative genomics of parasitic silkworm microsporidia reveal an
RT association between genome expansion and host adaptation.";
RL BMC Genomics 14:186-186(2013).
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DR EMBL; KB909361; EOB12381.1; -; Genomic_DNA.
DR AlphaFoldDB; R0KNY1; -.
DR STRING; 578461.R0KNY1; -.
DR EnsemblFungi; EOB12381; EOB12381; NBO_453g0004.
DR VEuPathDB; MicrosporidiaDB:NBO_453g0004; -.
DR HOGENOM; CLU_1778004_0_0_1; -.
DR Proteomes; UP000016927; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 1.
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; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF24; SERINE_THREONINE-PROTEIN KINASE; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EOB12381.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016927};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..114
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT COILED 17..44
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 146 AA; 16855 MW; E19C8F8CA9CCAB58 CRC64;
MVKGLETMIS LLNGKQLEEA SKQLEGSRKK MAQLKSEISM ARKSSILQTE EIPEDPVKLY
EFNNHLFSSK TFEQGTLCEH CNEVLYGIKD QGFECRDCKM VVHKSCYVLG DVSCEMYSAF
KTGETYFVMM RTIEEKEKLM GVYKKY
//
