ID E3M2U6_CAERE Unreviewed; 1127 AA.
AC E3M2U6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN Name=Cre-pkn-1 {ECO:0000313|EMBL:EFO89945.1};
GN ORFNames=CRE_07211 {ECO:0000313|EMBL:EFO89945.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; DS268422; EFO89945.1; -; Genomic_DNA.
DR RefSeq; XP_003109803.1; XM_003109755.1.
DR AlphaFoldDB; E3M2U6; -.
DR STRING; 31234.E3M2U6; -.
DR EnsemblMetazoa; CRE07211.1; CRE07211.1; WBGene00058472.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_132_0_1; -.
DR InParanoid; E3M2U6; -.
DR OMA; EVTINGC; -.
DR OrthoDB; 5400441at2759; -.
DR Proteomes; UP000008281; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05589; STKc_PKN; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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:SF242; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF02185; HR1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 2.
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; SSF46585; HR1 repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 799..1058
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1061..1127
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..240
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 828
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1127 AA; 126615 MW; 343E919345FCF661 CRC64;
MDYHSNGNGV NGTNGTSRFA AELPSTPPGN GFGNGEGSRY EKSANRFYGN VYDGSAPSTP
KSSLTTAFKS ACTNSPVVSF TRGVLRASRK KIRPLFTSTT TSSYESSYYR VPSPSHNFWP
DTTFFGPILA MRQPPPSQTL DIVDLDKSTY WEAAPAEMVE LANKYNFTID EGSSIQQEAL
ELRAVIRKDL KKKLKIKSGY SRIKLITSDR RQSEFLRFEL SDLNEQIADL QEDLQALEMY
NSGAFDEDVM YLDNLEDCDV ENGPPSKLLV LQLELEKELK VKRGLEQFLR GAPDKSKVHG
DSQSLLDDSR AKIAMLRMQI DRLSQESPAT EGDQKSKVEL AIEDLIIRYH KEKLIMDGSR
NMIRILRCQK KLDNKAIEEA LNSLIIASEK SDLIKLALLK YAASLPIEHK DRHSLIEEIN
AGRIPKPQSG SQDRNSPSSE EGSTSCSTAQ SRRCSFMPHS LQISGCLEVT INGCSGIISG
SFERRIRMDI PGMAGYTSVF GVDSTGKKKK SFKGPTSPDE VFCVLRIDNR YIGSSELKKI
IDRNWDQKFD VDLDRSRELQ IELFYHDDRS MCGFAAIKLS NLIETSTKVG IIVPVEPQGN
IFVQFKYMNP VVSRKPKLER QRRLFRVKES NDGARQKLGV FAFSRLIKSR GNEPSEKFAA
FTGFTPMASM SSQQQAGPSS SGPSSSISSV STTNPSTSNS LFDKVSNHLP GFNPRKSAKK
QREAKEAVLA SSAAAAVNAN LYVHPLTSVV PAPNRERSLV VDDYHAICTP GQSQAPVPAA
RHIDFFASSD GAPLTVEQFR LISVLGRGHF GKVILSQHNP TSNYYALKVL KKGDILGRDE
VESLMVEKRI FEVSSRARHP FLVNLHGCFQ TPEHVFFCME YSMGGDLMRH IHDDVFDEVR
GCFYAACVVL GLDFLHQHNI IYRDIKLDNL LLDRDGYVKI ADFGLCKENM GPFDKTSTFC
GTPEFLAPEV LSDSSYTRAI DWWGLGVLIF EMLVGEPPFS GDDEEEIFDS IISEDVRYPR
YLSVESIAIM RRLLRKVPEK RLGYGERDAE DIKVQRFFRH ISWEWDKLLS REIRPPFQPQ
IRNPEDVSNF DLEFTQERAR FSAASSTRPI TEADQRLFNN FDFSIVP
//
