ID B0WMV8_CULQU Unreviewed; 1194 AA.
AC B0WMV8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=6040685 {ECO:0000313|EnsemblMetazoa:CPIJ008013-PA};
GN ORFNames=CpipJ_CPIJ008013 {ECO:0000313|EMBL:EDS31350.1};
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:EDS31350.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS31350.1};
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:CPIJ008013-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ008013-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS232003; EDS31350.1; -; Genomic_DNA.
DR RefSeq; XP_001850042.1; XM_001849990.1.
DR AlphaFoldDB; B0WMV8; -.
DR STRING; 7176.B0WMV8; -.
DR EnsemblMetazoa; CPIJ008013-RA; CPIJ008013-PA; CPIJ008013.
DR KEGG; cqu:CpipJ_CPIJ008013; -.
DR VEuPathDB; VectorBase:CPIJ008013; -.
DR VEuPathDB; VectorBase:CQUJHB018098; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_007537_0_0_1; -.
DR InParanoid; B0WMV8; -.
DR OMA; HYKNTNL; -.
DR OrthoDB; 103262at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR PANTHER; PTHR22967:SF57; AUXILIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR22967; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EDS31350.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Transferase {ECO:0000313|EMBL:EDS31350.1}.
FT DOMAIN 1..261
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 399..575
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 581..717
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1118..1194
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 278..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 129289 MW; F1E8FE1A4743CF64 CRC64;
MGDPELDTAS GNEYALKRLL GADKEECNNI IREINTLKQV SGHPNIIRFV AASFIDRTQN
AGAAKRAEYL LVTELCKGGS LYDCLEKELA PDVVLRVFYQ ACKAVAHLHQ QTVPINHRDI
KVENFLLGGD GLLKLCDFGS ASTDTYAPDV SWNAHQRDML EDHLGRCTTP MYRSPEQLDT
WANYPIGVKT DIWALGCILF CLCYRKHPFE DSAKLRIINA NYTIPNDSRY ACFNDIIRGC
FQVDPVKRFD ISMVLDRLAA IAETKGWPLK APLALSGKPL NTPPSGPTPV PSPMHHQPDV
VPANHVPPAR PAPPRPAPMA GSAGPPPQER RNPQRPPDPV RPPPPVVGPA PVHHYPQPQP
GVAPGMVGAG GGLFSSIKGG AGSFLKNLKD TSSKVMQTVQ QSIARTDLDI SCITQRILVM
PCPSEGLEST YRTNHIEDVK IYLESRYLPT KISIYNLGPR SCPRIPPPVR TVEGNFIYSP
VPPSYKAPTL AGLYALAEDM YGFLNADPKT VIVIQSPDGG KALAATMVCA LLVYSGLCAE
PEDAMQIFAV KRTPPNMRAS ELRYLYYLGD VVRSVPHLPH YNPVTLVSVT LNPVPRMTKA
RDGCRIYIEV ASGDRILFST LQEYERMRLY GAHEGKITLA LNVTVCGDVT VTLYHARNAL
GGMGRPQGLK ICQFQLNTGY IPEEETLINF SKTELDDVPD VEHVPHGFNV ALSVFVGDSE
RPPASQPPWI PAKPVRDPKV LFASQLEYEE NVDNFISKPS GGSTKPAPHR PPPARPPAPP
SPQPARATPP IEIQDVPAAG SMPTDVDLLN ISASQQKKVE EAPPPAEQTT FDLLGGFAAP
VIDAAPATGS DQPTAGIDDI FGNFESAPGC GPAPLQSSKS GSELNGLNLN FDNFGGVAQP
AAASGPNGTN NQFNNSFGFD PFAGISASAF HSSHQPQQPQ PQPQQPASKD PFADIGNLAA
GLGATGPGGW GKPPPTTTPS PRSTQFSSPT HQFSGASTAN PSPRAPSTPS HQQQQMRSPN
SDPQRAADYS RSHFDQSKPA ANGNGGANGG GAKEKPGDIF GDILGSQGYS FGNMRNQGPR
TINDMRKEEQ IKEMDPERLK LMEWTEGKKA NIRALLCTVH TILWPGAKWT KCEMHQLVSA
ADVKKAYRKA CLAVHPDKHT GTDNESMAKL IFMELNNAWS EFENDATQQN LFAN
//
