ID B0WWT9_CULQU Unreviewed; 1398 AA.
AC B0WWT9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=6044331 {ECO:0000313|EnsemblMetazoa:CPIJ011538-PA};
GN ORFNames=CpipJ_CPIJ011538 {ECO:0000313|EMBL:EDS36200.1};
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:EDS36200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS36200.1};
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:CPIJ011538-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ011538-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; DS232152; EDS36200.1; -; Genomic_DNA.
DR RefSeq; XP_001861861.1; XM_001861826.1.
DR STRING; 7176.B0WWT9; -.
DR EnsemblMetazoa; CPIJ011538-RA; CPIJ011538-PA; CPIJ011538.
DR GeneID; 6044331; -.
DR KEGG; cqu:CpipJ_CPIJ011538; -.
DR VEuPathDB; VectorBase:CPIJ011538; -.
DR VEuPathDB; VectorBase:CQUJHB018391; -.
DR eggNOG; KOG0612; Eukaryota.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; B0WWT9; -.
DR OMA; ERDKYNQ; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20813; C1_ROCK; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05596; STKc_ROCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.730; Single helix bin; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51859; RHO_BD; 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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDS36200.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002320};
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 78..340
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 341..411
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 952..1016
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1121..1325
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1237..1291
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1012..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..623
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 652..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 804..831
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 860..999
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1029..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1398 AA; 160718 MW; 4245AEFFA6E51768 CRC64;
MTTLMDEDRR KRLLALEEKI RDPGSIANID CLLDTVTALV ADCDHDNVKI IKNIETYIKR
YKELAREIND LRMKPEDFLP IKLIGRGSFG EVQLVRHKSS RQVYAMKRLS KYEMITRSDT
AFFWEERYIM AHANSEWIVQ LHYAFQDAKY LYMVMDYMPG GDIVSLMNIY EIPEKWAIFY
TMEVVLALDT IHSMGFIHRD VKPDNMLLDK YGHLKLADFG TCMRMGPDGL VRSSNAVGTP
DYISPEVLQF QGAQGGYGRE CDWWSVGIFL YEILIGDTPF YSDSLVGTYG KIMDHKNSLE
FPGDAQISEN AKSLIKGFLT DRTQRLGRSG IDEIRNHPFF QNDVWTFENL RESVPPVVPE
LSSDDDTRNF DEIEKKNSVE ANFPTPTTFS GDHLPFIGFT YTGDYQLLSG GSQDNVDNKT
TSITGSHRNH HVRHRSSNNA ELLRMENMLQ RERNTIEMLE KQERTLRQQI ELITQRETDI
QNLANTYEKE LTMLKHNFRE MSRKADSEQE ARRKTEAQLL ETNKRLEEEK SKRTREMNNN
QQYNDKINAL EKQLTDMQEK YKSETEVSQK LKKQVAELRL SKTDVEQKAS DLASMLAGLQ
AARDALQQDV ADLQTRLAQE RNARIQMTEL QKELEGKLHS LGGDLERSVT REQQALEDNR
CLSDRISDLE KENASIECEL KAVQNRYHQE VRAHQETEKS RLLNNEEANM QEVKALQTKL
NEEKVARQKA EQNSQEKERQ ISMLSVDYRQ IQQRLQKLEG EYRQESEKVL ALHSQLEQEQ
SKKSTLLSEL SLQSSEVAHL KAKEMQLVKE VQQFRETKRK YEEDIVKIKN AHNVDILQMK
ELQDQLEAEQ YFSRLYKTQS NEVREELEEK TRQIQDLEEE RNSVLHQLTL AGARADSEAL
ARSIAEETVA DLEKEKTMKE LELKDLITKH RNELSTKEAA LTTLKDLETE LSKKLNNKLF
ELDDLAQQNR KMQDELGQLK SEQAEMEKLR TKLKTETMLK QQAVNKLAEI MNRKDNNLTG
GSKQKSKVNS AADLRKKEKE NKRLQQELSV ERAKYDELCL KHNDTISQLS REIDIKTKLQ
MEIECKATEI EHLQMKLNET ASLSSADNDT LEAADAANQP DAIFEGWLSV PNKQNIKRYG
WKKQFVVVSP KRIIFYSSEV DKQNTSDPLL IIDLSKVFHV RPVTQGDVIR ADPKEIPRIF
QLLYAGEGEA RRPDEQQQLD VSSSKADERP LTLQYKGHEF LQISYHIPTT CDLCQKSLWS
VFKSLAAYEC KRCRFKLHKE HVDNNNPLAP CKLHHDPNYA REMLLLATSN EDQNRWVSRL
SKRIQKSGYK ANSTNNLGGA GGGGGGGAGG STGSSSSGNG DGSKISPSQS TRSNYKPYAV
NVQRSATLPA NASLKQQQ
//
