ID A0A0V1D845_TRIBR Unreviewed; 1017 AA.
AC A0A0V1D845;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
DE Flags: Fragment;
GN Name=pkc-1 {ECO:0000313|EMBL:KRY57330.1};
GN ORFNames=T03_6621 {ECO:0000313|EMBL:KRY57330.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57330.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY57330.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57330.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
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:KRY57330.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDI01000032; KRY57330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D845; -.
DR STRING; 45882.A0A0V1D845; -.
DR Proteomes; UP000054653; 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; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR CDD; cd04014; C2_PKC_epsilon; 1.
DR Gene3D; 3.30.60.20; -; 2.
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; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
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; 2.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRY57330.1};
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:UP000054653};
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 2..140
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 474..521
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 545..595
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 685..945
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 946..1017
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 373..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY57330.1"
SQ SEQUENCE 1017 AA; 114437 MW; 37C7446DDB5AE011 CRC64;
LHCSTVLVLL GKNLLITIIM VAFTGSVGIR VIEAADLKPT EWSTRFSTLT TGLRQAGVAI
DPYVNVDIDE YRVGRTLVKQ KTSAPGWDER FHGKASNADT VGFTVFHNCA IPPDVFVANC
RLSFEDLQLG SNNLWIDLEP HGKLHVEVHL DGSFVDWQFG FGGVVRVETF AGERGHGVRE
TVVGHFGVAA QQDRRVISAQ RFDQFRKTAL QVRLGRRIQH KHQHAEPLAL GGRQRFGFGH
DLAVKIRVNR PRPRPGSARH FDELATEHRP AAVERLRPLA DRLTPVVRPG TEAPRRATHV
TVGGVAGGRF VHAQPAVFVQ VGQLVLEPVA AQRCHLLVEH AHLGRPRVQR RQPAASASPH
AFVRRLVGRI DPAELTPPVE NPTGYCSTGQ FHRGQRQNQT DHQKKPSRPG RLFPPKPTQL
SHRSPPLYPP LLCDTVSETK NATTSNRVFR EKAGAFIGRQ RRGAMRRRVH QVNGHKFMAT
ILRQPTFCAH CREFIWGIGK QGYQCQFVVH KRCHEFVVWK CPGVKDIGVA VGEFKSETRF
DINVPHRFEL HNYKMPTFCD HCGSLLYGIF RQGLQCQTCH MNVHKRCERN VANTCGVNSK
RMAEILSQIG ISGYSVKQKK KTSIMTLSER SRTDPLPIHS LSDDQTSSSS KSDECSINGT
LHFSMRHPAA AARRDSSSKF TIGEFNFIKV LGKGSFGKVL LAEKTGTDEV YAVKVLRKDI
ILQDDDVDCT MVEKRVLTLA AKHPFLTALH SCFQTEEFLF FVMEFVGGGD LMFQIQRARK
FDEARARFYS AEVTSALQFL HRHGVIYRDL KLDNILLDAD GHVKLADFGM CKEGITAEKL
TSTFCGTPDY IAPEILKEND YGASVDWWAL GVLMYEMMVG QPPFEADNEE DLFDAILQDE
VLYPVWLSKE AVSILKGFMT KNQFKRLGCV ETAGGEDAVR AHVFFKEVDW QALESKKVKP
PFKPKLKSKK DVTNFDADFT KEDPLLSPVD PLAMRMINQD EFKDFTFVNV DFHFHGR
//
