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Database: UniProt
Entry: B8M0V0_TALSN
LinkDB: B8M0V0_TALSN
Original site: B8M0V0_TALSN 
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
//
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