ID A0A0L0C6W2_LUCCU Unreviewed; 1018 AA.
AC A0A0L0C6W2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNC27977.1};
DE Flags: Fragment;
GN ORFNames=FF38_06179 {ECO:0000313|EMBL:KNC27977.1};
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:KNC27977.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC27977.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC27977.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC27977.1};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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:KNC27977.1}.
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DR EMBL; JRES01000835; KNC27977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0C6W2; -.
DR EnsemblMetazoa; KNC27977; KNC27977; FF38_06179.
DR OMA; HWEEYAD; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20795; C1_PKD_rpt1; 1.
DR CDD; cd20796; C1_PKD_rpt2; 1.
DR CDD; cd01239; PH_PKD; 1.
DR CDD; cd14082; STKc_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF24; SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000037069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 165..215
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 304..354
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 502..619
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 642..898
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 7..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 671
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KNC27977.1"
SQ SEQUENCE 1018 AA; 115006 MW; 339A7E6A73B83F7D CRC64;
VIALAAHFHH QQQQQQHHNQ TIPQQQQQQQ YQHHHHHHHP QQQRAGTGGI IANSSTVPNV
IMEGPEVTFL FQFGSIRDAV SVAANVLTLK TLKDLACEFI NTKIPDSGLT YLSERILLFR
HDYNSPNVLH IINSAGDVVD ETLVEIVLTA SPILYPTSDM PTLKPHNLNV HSYKSPTFCD
FCGEMLFGLV RQGLKCDGCG QNYHKRCVVK IPNNCNNSND LSNSSKRSSL LQPPRSPSGG
STQSLISNDE QQQQAKNDSG SSLNVPIYHR SHQRSSSAGS RNGQLLANTG ICATTSAYQN
IRIPHTFMVH TYGIPTVCQY CKKLLKGLFK QGLQCRDCQY NAHKKCMDKV PQDCTGERQL
SHGDYNESSY TPTHAAHKER DNFFKEEFDD SDFDDNASNE FNNSRTGYGG GNNIMAVKQG
RMGNVMSAKT TTNAHNSPPE LVNGLATTNE RTSYNRDSRC MAEGQSVDGQ SEQSSSSSSP
SANIPLMRIV QSVKHTKKRG GQAIKEGWLV HFTSLDSTVK RYFWRLDSKT ITLFISEQGS
KYHKEIPLAD IQLIETNNDV RVDNNYCFEI RTANVTYYAG QDPLAGVREE QAVRLPPPDS
GIGTDIAKSW ETSIKQAYMH VTNTQCCESE DNIQDMGQLY QIFPDEVLGS GQFGVVYGGV
HKKTKREVAI KVIDKLRFPT KQEAQLKNEV AILQNISHCG VVNLERMFET PERIFVVMEK
LKGDMLEMIL SHERGRLSER VTKFLITQIL IALKHLHSQN IVHCDLKPEN VLLSSDAEFP
QVKLCDFGYA RIIGEKSFRR SVVGTPAYLA PEVLRNKGYN RSLDMWSVGV IIYVSLSGTF
PFNEEEDIND QIQNAAFMYP PNPWKEISSN AIDLINNLLQ VKQRKRYTVD KSLQHYWLQD
KQTYRDLRNL EAQVGTRYLT HEADDMRWAS TENKQNTVST QPQQQIAETP LLEEQEKQQE
QQTPQPSEQE QLRRKSTLPQ LETIETCGCR SLPGKPKVEA IGDKALKWMR SHLCRHIK
//
