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Database: UniProt
Entry: B0X4A3_CULQU
LinkDB: B0X4A3_CULQU
Original site: B0X4A3_CULQU 
ID   B0X4A3_CULQU            Unreviewed;       442 AA.
AC   B0X4A3;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE            EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN   Name=6047421 {ECO:0000313|EnsemblMetazoa:CPIJ013835-PA};
GN   ORFNames=CpipJ_CPIJ013835 {ECO:0000313|EMBL:EDS40256.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS40256.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS40256.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ013835-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ013835-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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; DS232334; EDS40256.1; -; Genomic_DNA.
DR   RefSeq; XP_001864475.1; XM_001864440.1.
DR   AlphaFoldDB; B0X4A3; -.
DR   STRING; 7176.B0X4A3; -.
DR   EnsemblMetazoa; CPIJ013835-RA; CPIJ013835-PA; CPIJ013835.
DR   KEGG; cqu:CpipJ_CPIJ013835; -.
DR   VEuPathDB; VectorBase:CPIJ013835; -.
DR   VEuPathDB; VectorBase:CQUJHB006192; -.
DR   eggNOG; KOG0695; Eukaryota.
DR   HOGENOM; CLU_000288_63_29_1; -.
DR   InParanoid; B0X4A3; -.
DR   OMA; FIDWEAL; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05588; STKc_aPKC; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR034659; Atypical_PKC.
DR   InterPro; IPR046349; C1-like_sf.
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:SF216; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
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; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000002320};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..41
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          109..368
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          369..440
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          51..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   442 AA;  50878 MW;  043E604050014D15 CRC64;
     MKAFCAFCHD RIWGLGRQGF KCIQCKLLVH KKCHKLGSKP CSNEHVEPVL VQDPNDESSG
     QDGIPPPEQY PSGDSYHHEQ CDQVPVEVNE NVEEPLESGT QRQYSLQDFE LIRVIGRGSY
     AKVLMVELKK TRRIYAMKVI KKALVTDDED IDWVQTEKHV FETASNHPFL VGLHSCFQTP
     SRLFFVIEFV RGGDLMFHMQ RQRRLPEEHA RFYAAEISLA LNFLHEKGII YRDLKLDNVL
     LDHEGHIKLT DYGMCKEGIR PGDTTSTFCG TPNYIAPEIL RGEDYGFSVD WWALGVLLYE
     MLAGRSPFDI NTEDYLFQVI LEKTIRIPRS LSVKAASVLK GFLNKNPADR LGCNRDSAFM
     DIVNHPFFKS IDWEMLEQKQ ITPPFRPRLD SERDLANFPP EFTDEPVHLT PDDDRVIDKI
     DQSEFEGFEY VNPLLMSLED CV
//
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