ID O01669_HYDVU Unreviewed; 661 AA.
AC O01669;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
DE Flags: Fragment;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CAA72926.1};
RN [1] {ECO:0000313|EMBL:CAA72926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Zuerich {ECO:0000313|EMBL:CAA72926.1};
RA Hassel M.E.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAA72926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Zuerich {ECO:0000313|EMBL:CAA72926.1};
RX PubMed=9510545; DOI=10.1007/s004270050141;
RA Hassel M., Bridge D.M., Stover N.A., Kleinholz H., Steele R.E.;
RT "The level of expression of a protein kinase C gene may be an important
RT component of the patterning process in Hydra.";
RL Dev. Genes Evol. 207:502-514(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
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; Y12237; CAA72926.1; -; mRNA.
DR AlphaFoldDB; O01669; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR CDD; cd04014; C2_PKC_epsilon; 1.
DR CDD; cd05570; STKc_PKC; 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; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF240; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
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; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000551-
KW 51}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAA72926.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000551-51};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 1..117
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 172..223
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 243..293
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 369..628
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 629..661
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT ACT_SITE 493
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT NON_TER 661
FT /evidence="ECO:0000313|EMBL:CAA72926.1"
SQ SEQUENCE 661 AA; 75054 MW; 3346BD6EE4A2B2D5 CRC64;
MNGIQSGFTG FMKIRILEAL DLNKTNVKSQ FVTSMKVSSL DPYLQAYVDD QVIAKTSKKT
ATYCPVWEED FSIDLHKAKM LSLTVFHSSI VGSDSFVANS SVLIQDIIDE GQSDLWIQLE
PAGKLHIFIE LKSGEDGEPR ATSNQFKQRD STYLNKRGRR NAVRRRIHQI GGHKFMATYL
RQFTFCSHCK EFIWGVIGKQ GYQCQVCSIV THKKCHHLIV SKCPGVKIKE ETSSEQRYGL
NIPHKFLTHS YRFPTFCQHC GSLLYGIIKQ GVQCKNCALN VHRRCQANVA NDCGVDRREL
AERLKEINNK TANDIMKSPK PTNIIQHTQN GMTCITHDKT KPSIQDITAS PVDVCRKVAS
ETKYSLDSFT FLKVIGKGSF GKGYLAERKG SSELFAIKIL KKINIIRDDD VDCIQTEKRV
LTISGQHPYL TSLHSCFQTP ERLFFFMEYV NGGDLMFQIQ KARKFDENRS RFYAAEITLA
LQFLHKNGII YRDLKLDNIL LDSDGHVKLA DFGMCKDNLA PSDTTSTFCG TPDYIAPEIV
CDLPYGSSVD WWALGVVMYE MMAGQPPFEA DNEDELFERI QSSEVLYPVW LSREASSILK
GLLTKNYEKR LGCVPDIGEV AINKHPFFAS IDWRKLENRQ IHPPFQPQIK SPTDVANFDT
D
//
