ID A0A074Z7I3_9TREM Unreviewed; 1072 AA.
AC A0A074Z7I3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN ORFNames=T265_10146 {ECO:0000313|EMBL:KER21547.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER21547.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER21547.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; KL596958; KER21547.1; -; Genomic_DNA.
DR RefSeq; XP_009174694.1; XM_009176430.1.
DR AlphaFoldDB; A0A074Z7I3; -.
DR STRING; 6198.A0A074Z7I3; -.
DR GeneID; 20324314; -.
DR KEGG; ovi:T265_10146; -.
DR CTD; 20324314; -.
DR OrthoDB; 841660at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20835; C1_nPKC_epsilon-like_rpt1; 1.
DR CDD; cd04014; C2_PKC_epsilon; 1.
DR CDD; cd05570; STKc_PKC; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF201; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 179..310
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 365..415
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 429..450
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 605..865
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 866..938
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 482..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1072 AA; 119032 MW; 14C64A9054A2833D CRC64;
MHGEKGPENI MRIDAKKDLG IWVSSNLSFA LHHEKSAQKA FAVLRMIRRT FSRITRMDFQ
ILYGAYVRPL LEYANQVVYS GRTKDVTLIE RVQRAATRMV AGLKSVDYET RLATLDLFPL
EYRRLRGDLI LTYALFEQSL ANRFFTVDPA NTRRGHKPAF SNQSSLGGRQ HRCFHEYGNA
SLVDFTLHSQ RLPTMEYFSG TLNVRIIEAS DLKPTACATR HSLRPVAKLC ELLDPYVTVD
VDDIAIGKSS TKSRTNTPLW NEDVSAEVNY AQQLTFTVYH DAAIPPDDFV AIVEVAIRNV
RSGEDVWIEL EPHGKLHIRI DLSGTRTDEP PRDRLGFPSR DSAIGVHAKH YRCGAMRRRI
HQAKGHKFQV TSLKQFTFCS LCNSFIWGLW NQGYQCQVCT CVVHKRCYLN VITQCPGVKS
PPTGPTALLQ CEVCRLSIHK RCERNVASHC GVNTRDLIAA IRLCGLNPSD LGVIPTTSSI
GSIGSPTPSN AVSPGPHASS SSRPVSAGLR TSGIYGAYTD FGTGESRLTG SPIPLPPNVF
SENPIESDDM TLHSSGAAVL MSGPVYGRHG VPVARPSSLQ DPPTIHHTTT SSDVASIRIP
NLKDFIFLKV LGKGSFGKVM LAEQKGTGEV FAVKVLKKEV ILQDEDIDCT MTERRILVLA
ARHPFLTALY CAFQTEDRLF FVMEYVNGGD LMFQIQRARR FDEARARFYA AEVTLALMFL
HRHHIVYRDL KLDNILLDAE GHCKLADFGM CKEGMTPGKT TSTFCGTPDY IAPEILAESD
YGFSVDWWAL GVLMYEMMAG APPFEGDTEQ DLFNAISYEE VTYPPNLHPD AVDIMSKFLL
KSPARRLGCV AVDGGELAIQ CHPFFREIDW EILEERRIRP PFRPKVRSRI DTSNFDKDFT
NEEPVLTPTD HTSELTAIAK DVFAEFDCIN TDYSVMRYHT TRPSQQQPLR SMFSGAHLTT
SAVGTEPATS PEALSGGPTS PTHGTPLSNS PYKPASPTIT TPTVTTLPVT TPRSQLPFDF
PADSLVDSTT RLAITSISSA SQNRSVPSSP VHSHPSLPSF TERKVASKWL AD
//
