ID A0A0L0CNH4_LUCCU Unreviewed; 1143 AA.
AC A0A0L0CNH4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Kinase suppressor of Ras 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FF38_03748 {ECO:0000313|EMBL:KNC32984.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC32984.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC32984.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC32984.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC32984.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC32984.1}.
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DR EMBL; JRES01000249; KNC32984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0CNH4; -.
DR STRING; 7375.A0A0L0CNH4; -.
DR EnsemblMetazoa; KNC32984; KNC32984; FF38_03748.
DR OMA; DEGIPWI; -.
DR Proteomes; UP000037069; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
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; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 487..531
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 856..1120
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..190
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..736
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 882
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1143 AA; 125598 MW; FCE0EDF36F7D19A2 CRC64;
MEFIKKQIKQ SSLPKMSSVT TTPTKTMMTP IQQHQHSAMP SQHSASSHST PVRSPQPSSH
SASTSSLPAN DLDVIQDMID CSANRLEGLR TQCVTTTTLT QREIRSLETK LLRMFSELLL
TKGRLNERIP ASGLPHSSSN ELRQWLRVVG LSQDSLNVCL TRLSTLEQIL ELSEQELREL
LQNNPTYREE EIRRLTKAMQ NLRKCKDILT KPNESLQPAT LTGEGDKNNT STTAQSVINR
ETKEQLIEQL FWDSWDRHHR GSVGNIGVTA SPRSHRNMKQ AKQQQQLTNR QSPSNDNQSC
KSSSTTMNNS GEDNSVSALT LTLTPSPPHS PFTPTSTSTS FSNLGGGSSL NGTPQKGKIA
GTPPPMIKHA TALQGTQPLT PTHNSGGGGY QQQDHIPIPL AKSKSNESHS QDSPSLMANN
AGGGGAGSGG GLSRSRLNTD PSPDSHSSAS SDILMETSNN SSNNNSLQVP LSPLTPIVNL
SMSHNIAHRF VTLVKMATCD LCQKPMFIGR KCKECKYRCH KACEPYVPNS CCLPPEFIDE
FKQAIKDAVY PSQITPPTLN NQSPNQGHGT LGKGRKGLPS SRHKKHPSTA SSNVGMHDSS
SPGSSCNSSS PSSPALFNMQ HQHSSGDMQA TTIMSSSAGG SSTSSNMLST PSSHKNASQF
NFPDVTITSN CNNPSGATTE TILSAQNANN TSPNHEFSES HKSRNNSHEA LISASNNANT
HHHHQHQHHH HHHHSNTNSS NNSINVANTN NFTTSTSSTL TNHSSNSIVN VGPATFFQRK
LSSAGVDKRD NFAELSDTHK SNDSDKTVSL SGSTSASTDS DRTPVRLDST EDGDSGNWPR
QNSLSLKEWD IPYGDLQMLE KIGQGRFGTV HRALWHGSVA VKLLKEDYLD DEHMLEAFKL
EVANFKKTRH ENLVLFMGAC MNPPYLAIVT SLCKGNTLYT HIHSRREKFV INKTTLIAQQ
ITQGMGYLHA RGITHKDLRT KNIFLENGKV IITDFGLFSS TKLLYCDKGL GVPTGWLCYL
APELMRCLMP RKPSDEILPF SKASDVYSFG TVWYELLCGE FPFRAQPPES IIWQVGRGMK
QTLANLQTSR DVKDILMLCW RYTVEDRPDF PKLLTLFERL PKKRLARSPS HPIQLSRSAE
AIF
//
