ID A0A1Y2F9I3_9FUNG Unreviewed; 1399 AA.
AC A0A1Y2F9I3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=LY90DRAFT_29038 {ECO:0000313|EMBL:ORY80580.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY80580.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY80580.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY80580.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-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:ORY80580.1}.
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DR EMBL; MCOG01000012; ORY80580.1; -; Genomic_DNA.
DR STRING; 1754190.A0A1Y2F9I3; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000193920; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 839..1017
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1090..1381
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1112..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1399 AA; 162423 MW; 1F3A2448EA90A599 CRC64;
MAVPALTRRL NENEDQINAL YCLVEIALTN DTTVFRDIIN LLSEISKQEN YENNAKVKII
YQCFLIIART PNLPDKKYEV LLESLLFIFV SKTLLLPPKD LKHRRKIDEF TPLLIIIKEI
FSHDIIHTEI SCSNEMNIAF RNFWFYCILL GFRDGKWYNN WHTILNNIAR YTPTLLVSGS
NANSLETILE SNSILRQKFS DGLQALIKYE CSNMVTKNTE IKGLSFIQSA YLLTVHQLES
MRMDLLDITY IFQYILNEAT NNSGITNAMD VLADKILDIY LKKQEINIGT KEFTENIEKQ
IEFIVTNASH RLKRIRTFSR RFLEKMVTKF PSVLINKNTL YLMLNILIAL TSPLSIKSSE
KLFTDHSKIN DIVPYLELAD GCDHKKELAN EYLDLCKQWI EYASKVSSVE INGLLQSYLL
NIHIPTPGAQ RFIGTGVTSQ FGDMFGSKFI NSSFMNTFSL QSYCIGKVLG IRDAIKDNLI
SEDALLMQMK EKLQRFVKQY QLNDTALNQP EIEITKIVEQ FTSELYMVCA YIIVSKNVYK
DLIQDVCWIP VQMFHPQVMT VAKAAWIWLM TTRPELSLNI LIELLSAWEW TKYKQRGIFS
TNKIREDPFM HRITYTVPAK RKPKAHFAEV HSIWVEFLSD RYNVLKYNGN MYDKVFMKLI
QISFCNDNLS NSMYARKTTF QLLTLGMNVL HHQKQRPNDS KFELLLKKEL YEVAFSWFKD
PSAWGDSNDR QTLENEIKAI DEFCQCVKMD VKYNLTSMKN LNKFKHTGII FKILFQQYSK
LTYEQFAKNV IKIFENAQEI LLLLLEDELR HLDIWYDPER KLQNKVNIPA RLSYNKNKWG
TLISSAWNIS PSLAAEIPNK FKLPVLHTEL IRLITSNPLA VINSTSALEE VINQKCNISS
NYGFRSLLYW TQVSPIHAIS FLANQTEKNP WEIQYSLRVL EHFPPDMIFF YVPQIVQLLR
NDPLGYAEHY ILKTAHSSQL FAHQIIWNMK ANMNIEEKDG TQVPDKIKPV LDRMIEKIVN
PLSGADKEFY EREFNFFNEV TGISGKLMPF IKCSKPEKKK KIDEEMAKIK VDVGVYLPSN
PDSIVIDIDY KSGIPLQSHA KAPFLATFKT KPRATGEGEN NYEENDSESD DENNKEIWES
AIFKVGDDCR QDILALQLIA IFKSIFVKDG LDMYLYPYRV VATETGCGVI ECIPNSISRD
QMGREKVNSL YDYYVVKFGH SDTVSYQKAR ANFIRSLAAY SIVLYMLQIK DRHNGNIMFD
NEGYIIHIDF GFILDISPGG VNFENVPFKL TGEMLEVMRE EIDQQPYEWF CELCIRGYLA
IRPYATQIIE MVTLMQESGL PCFRGEVTLK KLKQRFQLDL TEQAAADFMS ERIKESRQNI
LSVGYDLFQQ IQNEIPYHR
//
