ID A0A2I2GN35_9EURO Unreviewed; 1951 AA.
AC A0A2I2GN35;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=P170DRAFT_397579 {ECO:0000313|EMBL:PLB54298.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB54298.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB54298.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB54298.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:PLB54298.1}.
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DR EMBL; MSFO01000001; PLB54298.1; -; Genomic_DNA.
DR STRING; 1392250.A0A2I2GN35; -.
DR VEuPathDB; FungiDB:P170DRAFT_397579; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000234275; 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; cd05167; PI4Kc_III_alpha; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PLB54298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1370..1556
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1643..1935
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 477..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1951 AA; 216690 MW; 262FDB32874768CC CRC64;
MDDFSADIRF SAFEKLATLA VQSPASDEES DIARLSRHYK QLVHCSSGLN GTLRSQAPTS
RVPMGIRELD VLVALCKASS SVNRLEHASR LVMQLSQYLP ESHSQLFRPS PFLHNVKPSP
WEALTFNITS ALLRLGLEYP SLHDKVGIAV NGYLDNCAEA INVAVPLLNY GSGAEKQGAV
HESVGVLSIA VSLVGFLEAS AMFTPFWDAT KQLQILQQLR SILSEGFMIA VETASSTVRH
AGTSEHGLRD WRKYTRRYSA DGRPLGAMLL QAGLMQFVKA CATSLVGAQN CSDSELLDDY
MNGVGIARSH DEAEVNLLDC LTEAIADQIQ LLDDGSDYLQ LGSPLQQKLA FSVKAYAFIG
YLQCVILSGN ITNSEDFQGW LEDVLMDPNQ MSCSELATAT LKSIAIVAKM SLSGAASGSR
SLLRYIVEGG VSSRSSSAIS AKCLAQVLGI LSQDAVITTL YSLGNVLSPG SGSENIYNGQ
PVTEASGHGN TGLPSSRRRN GSVASISLDG EEVIPYRSVV HAIVTIATNC RDEKISALAQ
SMLLQKIGKI NAAVDAYIIK ETASLSLSTG QAEFQLLLKF YDRIYWDGVI KGHDNVTRAV
QSAMAYLSVS LQKDSPLHRV YLVHLLESIV NKGDATDFEN ERQKDIVLAP NDIVPLLKPL
ALLVSSEKAA GAGEVVVEYD QVVSSLFRDA WFNLAIHGMS LSSAVVQKHH KVLRLLAIYS
PPLVSEDRME MLESDVELNT ILRRGMGPQR HLEQKKMLIS EIPSRESDIK RLNYPRSVFL
NAVLLIECLR ASSGHCTKIL DYFRDPAVAT FEMASCMGDI AEKIISDYLS LTLSGKHEIF
SVPFLSKELA GFFVACCHRI ERVQNVAVVC ANKIINECPS ALCAKHSLFA LLELLTVMWN
SCLEEDMDEF EWKPSFTSPM GIVTVDLPDN YVYRRKTLNV FLERATAWVT AVMNVAPLDI
KGLLQTYLSM PDDGTGFGQV SMGRSFAVNM GSLIPKSDQR LGSLETHTVG VTNVASDFIG
QYSTRQKYRF SDALSVGNGR LAPGNIGPNV STSSITLSES SREIESVLSE LHQKVKQRND
MSLVEIRDTL RRAAAVLCSS SHPHPSIPHY LVSLPFETFS EESINMGISL WMGAIHENPR
VEPMVLVEVL NAWERTIERK RGLFDPSFDY VDPMYAKIEL LPTDKALILS KQQDAQAHLA
PHLHILRFFE SHFSAIRLGN AQSQRLFCRL VDRTTAGLAQ TSGHPLAREL HFRIVLFGLN
VLGHSNSVGM PCLWKLKDQI LSGALSWFKH APRWSFGGNR LQIKTEDKIL GDVISTLGTT
ASISCDTHGP YKSLQAKQNL LLVLLENERS RLKVWLYPLD PDRKHYISQS PTNRNHTEEA
TSLLRLAWAE SSGLAIQLAT RFPSSKLKND IRWLLLNFPE KVIDEPSGLE IMFGEALPAD
VSFQLKYLLY WAPVNPTEAL TYFLPAYGNH PFILQYAMKA LESHPIDVRF YFVPQLVQAL
RYDALGYVER YILETAKLSQ LFAHQVIWNM KANSYKDEDS QVPDPLKPTL DKFMDDLVAS
FSSEERSFYE REFSFFNDIT GISGKLRPYI KRSKPEKKEK IEEELRKIKV EVGVYLPSNP
DGVVVGIDRK SGKPLQSHAK APYMATFRIQ KTKPVALGPT TPVAHAPDPD SADDRKQETY
EVWQSAIFKV GDDCRQDMLA LQMIAAFRSI FTSVGLDVWV FPYRVTSTAP GCGVIDVLPN
SISRDMLGRE AVNGLYDYFV SKYGGEDSIR FQEARTNFVK SMAAYSVISY LLQFKDRHNG
NIMVDDAGHI IHIDFGFCFD IAPGGVRFER APFKLTSEMV AVMSGFGLAG GGSHNPTTTQ
PYRWFESLVV KAFLASRPYS TRLSHIVSLM LDSGLPCFKP DTLKNFRDRF ALDRSEREAA
EYMRELVRKS YMSVSTKGYD QFQLLTNGIP Y
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