ID B8M0V0_TALSN Unreviewed; 1980 AA.
AC B8M0V0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=TSTA_089670 {ECO:0000313|EMBL:EED21730.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED21730.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; EQ962653; EED21730.1; -; Genomic_DNA.
DR RefSeq; XP_002478693.1; XM_002478648.1.
DR STRING; 441959.B8M0V0; -.
DR GeneID; 8104934; -.
DR VEuPathDB; FungiDB:TSTA_089670; -.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_1_0_1; -.
DR InParanoid; B8M0V0; -.
DR OMA; TIEVWQS; -.
DR OrthoDB; 147843at2759; -.
DR PhylomeDB; B8M0V0; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
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; 2.
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:EED21730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EED21730.1}.
FT DOMAIN 1374..1549
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1641..1964
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 24..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1851..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1851..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1980 AA; 221799 MW; 2D0868ECCAA208A0 CRC64;
MDALTPGLRR KAFERLAFLD TLGSQENSSK PSVSQLINEC RPQSSQSGGF KDGFSQGHGK
APMALRELEI ILSLAKTSAN VTRHDQMLNL TSQFAAHLTE SYSQRFRASP FLHDIKPSPW
EALTHGLTTG LLNLGQKDTS VREHANSAIM TYLNNCARAV KGMVKGGTER SEFEGAIGPV
EILITTLSLV GFLEGASHFT ELWNATEKLA IIELLESILS VNLLVAVETA ASKIRNSNAI
DPTSREWKRY NRRYAAHRRP LGAMLLQQCF LRFIKSCTVT TVLGHAAPTD VSFLEMYADG
IPLVKTSNEA EEALVKHLVG VLTDRIQLLE DGADYLQIGS QWQQELAFSV KSSSLIAFLN
CMTLNEKLAD TDLLLSWLED TVADENQMAA FDLGTTALKV VASTAKQFPA NASNLSHLLL
KFITQGGASQ SIVSVAASCL ASILEVLSQD FVITTLYSLG NVLSPTAAGV ERPVQLPVET
SENGPSVDPY HSNADSVISL SYNSEEDSTL THRNVIHAIV TIAVHSEDEN IAALAQSMLL
QKIGRISVVA DAYIIQETAA LALVNKHSEF QLLLKFYTRL HQEALLRGHT IIIDAVHNAR
NRLSVALRHS PPHKATYLMH LLESIISKGD VSDLGQDRHK EITLSPDDIT PYLKPLAFLV
SADEGKESGS IETTQYDEDT AALFRDTWFN IAVHGISTQS DIGRRYRNEL CAIAAKSPPL
VPENRTEILE SDVELNIILR RGMGHQRLAE QKKLFSSELP EHEASLKRIS YQEIVFLNAS
LLIESLRASA GDCTRILLYF LDPTLSSTEL GKYMKAVVDK VIDTYLSKTL SGIGERFASP
HLSKQLAEIF VTGCHRIHRV QEVALDCASK IISRSPSVLC DRSPLFALLD LLTIMWTSCL
ENDLDEYGWQ STFTKGDVTV ELSDNHESRK RTLDLFYSRA KSWMTVAINL APLDVKGLLQ
TYLSEYEDDG AYGHISLGRS FALEMASQIP QSDQRLSHIE RYGADNVNCA SDLIAQYTTR
QEYRYSEFSQ ANGKRKENAQ TNGTVDPYLT QYIEAIENLL KQLSLRASAG YDLSSHELQD
ALRKAAALLC RSYDDLPSIA HYLVDIPFQI FTKESIKFGV SIWLGVINEN PKTEPRILAE
VASAWESTTL SKKGIFSPTF THPDPFFTAI ELLPSDKTAL LRKQQQAQDV LSPHLRILQF
FESHFNAIRL ASPHLQRIFS RVISRTLVAI QCTNGHPLSR EVHFHIVLLG LRILQYSTTQ
SRAYKWKLKD LILSAALSWF RHSPRWSFGG NRLQLKAEDR VLKDVEDALK YAANLSSSNL
GRRQSLRNKQ ELLQLLIENE RMRLRVWLYP LEQEKKHYIT VFGSKSQSET GIIDQLLHTA
WAENPSLAIQ ICTRFPSQKL HDDVRRLLLD FPEKAMGVPE SLEMMFGTSL PADVTHQLKY
LLYWSPVSPT EALTYFLPAY GNHPFILQYA MRALESHSID VRFYFVPQLV QALRYDALGY
VDRYIYESAK LSQLFAHQVI WNMKANAYKD EYSEIPDAIK PTLDKFMDRL VTSFSDEERD
FYEREFSFFK EITDVSGKLR PYIKKSKPEK KQKIEEELRK IKVEVGVYLP SNPDGIVVGI
DRKSGKPLQS HAKAPYMATF RIQKTKALEG KPRAEQIQSD KENSHDQETY EVWQSAMFKV
GDDCRQDILA LQLIAAFRSV FNSVGLDVWV FPYRVTATAP GCGVIDVLPN SISRDMLGRE
AVNGLYDYFV SKYGGEESTR FQEARTNFVK SMASYSVISY LLQFKDRHNG NIMIDDAGHI
IHIDFGFCFD IAPGGVRFER APFKLTSEMV AVMGGGPHLA GSSSNGSITN GISTGSINTS
NGAGSSPAGS SALRLPIPGT HSHDPTTTQP YQWFESLTVK AFLASRPHAT KFIQIVTMML
DSGLPCFKPD TIKNFRDRFV LDKTEREAAD YMRELTRKSY LNISTKGYDQ FQLLTNGIPY
//