ID E4YKV1_OIKDI Unreviewed; 447 AA.
AC E4YKV1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Protein kinase C {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSOID_T00028595001 {ECO:0000313|EMBL:CBY36112.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY36112.1};
RN [1] {ECO:0000313|EMBL:CBY36112.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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; FN654725; CBY36112.1; -; Genomic_DNA.
DR AlphaFoldDB; E4YKV1; -.
DR Proteomes; UP000011014; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR PANTHER; PTHR45729:SF10; PROTEIN KINASE C; 1.
DR PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 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; PS50004; C2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 21..69
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 82..129
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 136..254
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 298..447
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 447 AA; 50782 MW; D73525869E6E9D51 CRC64;
MTKPKRSRDK IRKRSVRSVR GHECNDTMLK LPLFCDNCDE FIFGNDAYRC RACNVIIHKP
CISKEKVNLG VDHGRAAEGS TVHEYRERVV KNPAQCDQCG VLYENKVFHC AHCGIRAHKD
CLNFIPSTCG MAGDQLRGTL RITTYFDDNR LTVHVHEAKH ITAMDVNGKS DPYVKISSYH
KAGGWSDGSK TRTRKKTLNP NWNEKLVVFL DTDDSDCRVL IEVYDWDGFS DDDLIGGFSI
SGNELVKNSA DGWYRLLGKN ESVFYNIPVS YSKEKMARIW EEMDDDEEDE SGVSITDFKI
QGSLSSGFFG QVLLAINEEE EKVAVKVMSK YKVTSSGATG DVFAERDIIK LASPHIVELF
RAFQDTENLY FELELCEVGS LLDVYEFYEG EISSISSKFI LAEESFHKKH IFSKFYFMKR
NKRPFAPSSF YMASTLSTET SSLATFS
//