ID J9DPX2_EDHAE Unreviewed; 2110 AA.
AC J9DPX2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=PI3K/PI4K catalytic domain-containing protein {ECO:0000259|PROSITE:PS50290};
GN ORFNames=EDEG_01179 {ECO:0000313|EMBL:EJW04595.1};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW04595.1, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW04595.1, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW04595.1,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:EJW04595.1}.
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DR EMBL; AFBI03000016; EJW04595.1; -; Genomic_DNA.
DR STRING; 1003232.J9DPX2; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_01179; -.
DR HOGENOM; CLU_232252_0_0_1; -.
DR InParanoid; J9DPX2; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000003163; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00893; PI4Kc_III; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000003163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1842..2094
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 741..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2110 AA; 242275 MW; 1617F713A64B8195 CRC64;
MKDDPKLWLF RLFNSPYFDT WLTISYLYRY PNNGIQYYLC RKLKQLPLEK RDYFEKCLPH
LVHIMLSNST KTKDLSTTSC NSCGSTDSYS LSCFETDDCF SKLVYKYDNP FNYTTETSRT
NDNVCNVYYN EPNNRVSLNS ASNSNECCSI SDICNNNVLF DDNILANKPK YCINCDFIYD
YKYSFSLYDL LKDGGIEVYF MVKGASDEYG FICEVLCSEI LQRGFALKYY DTKMLNKNID
SNLSNSVVPE SSTYENNNYD KYASSFKDKN DRYGSSRVMK RSYSTDNYLE TAISQDTEIN
SIIYKNSLDY LGNQATNPCS ETCSVKSDNT YLSSLFIDKR RSRPSSNNSL INAMVSDNAK
STEHIPDIDV STNKCNLKKL TNERETLNNF GSYKFEDLRV NNNDIVCGID KMNIKTNTTI
STQINNMKNI SNINNTNNIN SINNINMSIK SVDYLRYYKN DLINILDKDD TKKTKLPIYC
SYNLLTEPKI PSLPRKCLSI QGIFTFFTRV VSGFFFDTTE LVNYENIFYV PLYRKTANTI
FTSLPRDKNV ESCKCDIVKD NNKGEFLSST QSSVNADSFN DNYFILKDDD NDLENRESYY
NNKSIFDSNT SKITLFNDIS INNKSKKIQM CNKINVNDIY LKPSKVNICN DIDINNDKFS
DINVCNDTEN NDVLNINSVA NKDNKLKDFD SNNFSTDIIP TNNILPINET ILDSNIKSNM
TTSTFKGNQI NELEEFLTPN KKSTKQGIDQ QSKKCNQNIK SKPNNNKSHS SKKKIVKSKL
IVIKDEGSSC ENNSSSTTNK NHENKKKSKY SMKYLFQGFI GSKNIKSSEN ASNFNINSIN
NTNENSDSTD NNAVLCSIDD NSNPCINNDD SIIDNNDNID DNTVFNYIDN NMIDGNLDNK
KLNSYKNYKK SESNIDKNKI DTNIIIDNIN DNGIGKKIDL LEKSRTDEFG LKSNIKVPKL
SISTIECNTD TPSINKISDI SCNKDDKDMS NNNKPVLIIK STSVIQKPTD VKNETFDGVN
TEFGNTEKND KNIKNTKLDN NININTSNIN QNVTDDFNVQ SVDGNYENSK KVVTFSSDII
RFYPNVIEIE DSYSILDENN KIIEPSDKMS LNSVDSKNNN ITEVNTDSIE SNKTNDNSLD
IENKEEMHNF KNNIDNKIIH EHKQPMECIE AKVYVENINN NISDRKNNIN KFCNKECAMN
ISHNKICSDN NRSINDNIKE NCNESNIDNV NIDNSNDDHI KDNKNINTNN IKDDGNKNNT
GNVKKSSNNI YIRNTKEIEP ENTKNNCSHN SKNTDSNNRN NKEHVNTHTN LKKNKKNYIQ
NTDIIDKNNN ADLTAGKIAL NIHSKNLIIT SEKNNRDINN NSTENLMESY IPISSVDEKN
NINVLDNILL DSRSATDSIE LSEENKVSIS SINENKKIML KNDDNKKLII ENDININTIP
NIDDINNNKF LSIIEKDNMK PKIILSKLEN NQQTEIQKIN KIDSDSNIDS NLNLNNESQK
LKEKTFVIEN SDLSVNVDKK NQPNIIIEQF KNTQIPSFTK THVDVDSKNH LKTRQKTHEK
NIKMLYLNPF GDRKNYRSNK SSLLFRGLLF KSSFKSILPS VLFLEELVTI CKRLKTLPRP
LRQRGLEIEI DLLNYNIQNS INPIDIPLSQ STVVNIVKEY SAILDSAENS PFYVVFETYD
KNQICNTCKS KYYSNDIRNV KYICNNIRDT GEYDNMTSQN CQNNNLNKSN NNAETNKINN
NLFNDEDPNQ YNNIYLDHTC FRKLKKQPSE IDNEFSLKNS PQNKEKDIIN TNFKNAAFLL
HKLYSLTKDS TLAQNEVNAI KERILNTLNQ EKSQQNRPNL TWPQKKELIR YNSIYKNYKG
YKIIPAIIKR GNDLRQEILA LQILNEMKSI FAEEDLHIKL FTYKIILITN KSAFIECIEN
VESIHTIKKK HTLIEYFKKV IAKKVGYDNG IDNFLCSLVG YSLATYLLQI KDRHNGNILI
KDDGQLIHVD FGFILGTHPG FYNVERAPFK MSTEYLEILG SKMDIFKSTF IEGFMALRRN
SDRLCRIIEI VSVNGYVSKK NIQAFRERLK MDMGDGDVER YVEGLIGWSI NSIGTGLYDS
YQYFSHGYLK
//
