ID A0A0V0X5I9_9BILA Unreviewed; 985 AA.
AC A0A0V0X5I9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=Pkn2 {ECO:0000313|EMBL:KRX83276.1};
GN ORFNames=T06_5669 {ECO:0000313|EMBL:KRX83276.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX83276.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX83276.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX83276.1};
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KRX83276.1}.
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DR EMBL; JYDK01000014; KRX83276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0X5I9; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11622; HR1_PKN_1; 1.
DR CDD; cd11623; HR1_PKN_2; 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; IPR037313; PKN_HR1_1.
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; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 3.
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; 3.
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.
DR PROSITE; PS51860; REM_1; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX83276.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 123..204
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 207..289
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 656..912
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 915..985
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT COILED 137..201
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 685
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:KRX83276.1"
SQ SEQUENCE 985 AA; 112040 MW; 9577A56FFBFA2A2F CRC64;
LFFLSGLLRP FQGVTMAHSQ IPDQLMLLSK KYGLVVNQEP TSADENALQQ LVSKLKKLIR
SLIAREMRFK EGYENMRRAV KDKKQVDALK KNLRSISDKI EDLHSDLFTI EMYATGTADL
SSASSTSDFN DSLNISNAAI NQKLAGLTRE LERESKVKDG LEKFLQMCKD KKMLEGSRQM
LEDSKAKIEL LRMQIARLQQ LHSLNLSSPV EGASPVASPT EIQVDELLHR LRKEAAMHEG
AKNMVKILNQ AKTVEKKSLQ DALDSQLESR EKLDLIRLAL EKHCQQLPTH SPKRESVKTD
IVQSNPSLYR NRTEELPDDA AAANASSQLL LNRHCAASSL AVSGKLEVRL MGCQKLLVDI
PGRAADSSAA AAEPGFSQKK TRSVGSRANT YRLKDNLSEE IYAVLRVDGR KVAQTEPKPY
SQQAWDQRFS IDLERSRELE INVYWNDWRS MCAFTFLKLG NLIDSYQDGR VVQLEPQGTL
FADIRYLNPV ISRKPMLQRQ QKLFRVKAQK VLPVRPGQMH VAAWGRIIKQ FFPQMCQDVP
AHASSPPSGA MNGRASRLIT QRSDSSLLND SLPYVLSPAA ISETSTSSLY PSLKEFGDQD
RKYSFPSSST LIDDRLVQDV KKLEKETLSL KLSARNLNAS SGYRQSTNAT MTIDDFKLIS
VLGRGHFGKV ILSKYRPNNN YFALKILKKA DILSRDEVES LMAEKRIFEI VNRSKHPFLI
NLYACFQTRE HVCFVMEYAM GGDLMRHIHD DIFTEERACF YAACVTLGLQ YLHDNKIIYR
DLKLDNLLLD RDGYLKIADF GLCKENMGFE DRTSTFCGTP EFLAPEVLSE SMYTRSVDWW
GLGVLIFEML VGEPPFSGDD EEEIFDSIVN DDSFFFKFTI CDYLFQLLRK NPAKRLGSSE
ADAEEVKKQR FFRLIDWQWD DLLAKKLKPK FIPTIRNQED VSNFDEEFTK EAPLLTPPKD
RKVVSNSDQA YFKDFDYLAD NSCIV
//
