ID Q8ISD9_DROME Unreviewed; 966 AA.
AC Q8ISD9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE SubName: Full=Kinase suppressor of ras {ECO:0000313|EMBL:AAN17651.1};
GN Name=ksr {ECO:0000313|EMBL:AAN17651.1,
GN ECO:0000313|FlyBase:FBgn0015402};
GN ORFNames=CG2899 {ECO:0000313|FlyBase:FBgn0015402};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAN17651.1};
RN [1] {ECO:0000313|EMBL:AAN17651.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12694293; DOI=10.1046/j.1365-294X.2003.01741.x;
RA Riley R.M., Jin W., Gibson G.;
RT "Contrasting selection pressures on components of the Ras-mediated signal
RT transduction pathway in Drosophila.";
RL Mol. Ecol. 12:1315-1323(2003).
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DR EMBL; AY135099; AAN17651.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ISD9; -.
DR AGR; FB:FBgn0015402; -.
DR FlyBase; FBgn0015402; ksr.
DR VEuPathDB; VectorBase:FBgn0015402; -.
DR HOGENOM; CLU_006812_0_0_1; -.
DR ExpressionAtlas; Q8ISD9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; TAS:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; HGI:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd20812; C1_KSR; 1.
DR CDD; cd14063; PK_KSR; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.10.140.1120; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025561; KSR_SAM-like_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR046861; SAM_KSR1_N.
DR InterPro; IPR046933; SAM_KSR1_N_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR23257:SF780; AT08303P; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF13543; SAM_KSR1; 1.
DR Pfam; PF20406; SAM_KSR1_N; 1.
DR SMART; SM00109; C1; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 371..417
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 679..943
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 966 AA; 105784 MW; EC8E3A8B9FB9FE42 CRC64;
MSSNNNAPAS APDTGSTNAN DPISGSLSVD SNLVIIQDMI DLSANHLEGL RTQCAISSTL
TQQEIRCLES KLVRYFSELL LAKMRLNERI PANGLVPHTT GNELRQWLRV VGLSQGTLTA
CLARLTTLEQ SLRLSDEEIR QLLADSPSQR EEEELRRLTR AMQNLRKCME SLESGTAASN
NDPEQWHWDS WDRPTHIHRG SVGNIGLGNN STASPRTHHR QHGAKGKNSA LANSTNFKSG
RQSPSATEEL NSTQGSQLTL TLTPSPPNSP FTPSSGLSSS LNGTPQRSRG TPPPARKHQT
LLSQSHVQVD GEQLARNRLP TDPSPDSHSS TSSDIFVDPS TNASSGGSSS NVLMVPCSPG
VGHVGMGHAI KHRFTKALGF MATCTLCQKQ VFHRWMKCTD CKYICHKSCA PHVPPSCGLP
REYVDEFRHI KEQGGYASLP HVHGAAKGSP LVKKSTLGKP LHQQHGDSSS PSSSCTSSTP
SSPALFQQRE RELDQAGSSS SANLLPTPSL GKHQPSQFNF PNVTVTSSGG SGGVSLISNE
PVPEQFPTAP ATANGGLDSL VSSSNGHMSS LIGSQTSNAS TAATLTGSLV NSTTTTSTCS
FFPRKLSTAG VDKRTPFTSE YTDTHKSNDS DKTVSLSGSA STDSDRTPVR VDSTEDGDSG
QWRQNSISLK EWDIPYGDLL LLERIGQGRF GTVHRALWHG DVAVKLLNED YLQDEHMLET
FRSEVANFKN TRHENLVLFM GACMNPPYLA IVTSLCKGNT LYTYIHQRRE KFAMNRTLLI
AQQIAQGMGY LHAREIIHKD LRTKNIFIEN GKVIITDFGL FSSTKLLYCD MGLGVPHNWL
CYLAPELIRA LQPEKPRGEC LEFTPYSDVY SFGTVWYELI CGEFTFKDQP AESIIWQVGR
GMKQSLANLQ SGRDVKDLLM LCWTYEKEHR PQFARLLSLL EHLPKKRLAR SPSHPVNLSR
SAESVF
//
