ID A0A0C9Z0S0_9AGAM Unreviewed; 1697 AA.
AC A0A0C9Z0S0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=PISMIDRAFT_86006 {ECO:0000313|EMBL:KIK31060.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK31060.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK31060.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK31060.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; KN833685; KIK31060.1; -; Genomic_DNA.
DR STRING; 765257.A0A0C9Z0S0; -.
DR HOGENOM; CLU_000893_0_0_1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000054018; 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:UP000054018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1133..1319
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1420..1684
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1697 AA; 190889 MW; 4A0A3652A79C8800 CRC64;
MEMQWTVLAQ SLISSEGIPY DGLPREAAAA NKAWSTLMKQ AANKVTFHGE TVEALRSTVK
GALQCFNDLL GQMEVMDTEP PLDTYAWETM SESLKLASIC CVAARELDPD LYSSLGLLLS
DKSPIVDNLV QEAALKSTTV IVQSFTEIAG ELVPHLRRFV TSPLPIFEFA FNSEKRAPPP
LTAAAKCFAL CIKLAPGEDS IMSNMYSLLN FFAAISKEVT ESSSQQLLQN PLYGSSYASS
ADQFSYWSEE TGLRGRSDEE KRLIGITTIS IAARLALEFD KEEVTKLTIS MLLQRLRIVE
PTLEAALVYN LADLALVAPV DAFRDIVKAF SSINRVANSD DPRFSNNMVL AAQTRLAREL
DRRPDLYDIY LEELLTLFSD KGVAIQNAAS SAHHAKTEEM IEQLASLLLP IEALLNHADF
SPLANASPEL LTSLFRNMWL LCVLLNITFT EDKEREKSAM TWLVPALGRI ATKTPILVLE
SATDVLSDLE YNTNVRHEYA RSVISKHRAC LARYIPMRAS EIRSLSAGQV LFVLAMHDVE
TLRSDAGLPS SLVSYFTNPS LNKHVALSAC MEAVAEKAYC VSSLNIQAAE QALPIHLSYE
LRDLLVFSTH RVARAREVAN KYLNRLITSF PSLMCDPTLV YAILECLTLL RRACDGEFID
EYSPRYEFYS ERTGISLQLT DDYKVRNDIL SQLRKSAHNW FELALGRAPV ELQSILQKYL
AATHSLTGAD TAELGASVAE QFAKAYGPVH RQLTALCSLS HWKSDRSRVL ASQLASKGYY
AGEAAGLRLA CYEGKDVLDK NPPQRTSATV IEALKKKMEE TSVGISNKNT GLMVQDLKRL
LFRCAAILIS LDECDHNLLH RLVTLPFEVF TPIAIATGIE VWTWVIAEKP STEVALMSEV
LSAWFGTVRE RRGVFSQSLN YQDPFQHPIG YVPTDKEEID RAATTAQRLL VPHTLILQML
FSRLQSARYR RSSVMFLIQR LVMRSACAHR FFSTHPLARE LRFSFLLFGF ETLKSSHLDA
YCEGLVRRSL YRTAYSWFAV QPQWSYGANR VQVTADIKIL QEFLTHLQTD CVKGFNSLSS
LALGQSPDQS SYVAYLKNIN HPLRLLVENE ITRLTVWVNP SNESGRGTDY HSNTERTMLD
NNWPTCVRTV WEIDPAIALH MMERFKSPSA HVEVERLVRA NPMAVASTPE GLKFLVDDKG
LIHQKNDLQY ILTSAPVSPV IAVTFFEKKY NDNPHLLQYA HRVLKQHPVE LTFFFVPQIV
QALRFDDLGY IKQFILETAK LSHQFCHQII WNMKANCYKD DAAEIEDPMK PLLDGMIDSI
VKSLTGEARL FYDKEFSFFH EVTSISGKLK PFIKKTKPEK KAKIDEEMAK IHVEVGIYLP
SNPDGEVIDI DKHSGRPLQS HAKAPFMASF KVRKSRTVVD SDPEALLDDN EVEKHEDYEI
WQQAIFKVGD DCRQDVLALQ LIAMFKNIFT SVGLPLYFYP YRVTATAPGC GVIDVVPNAT
SRDEMGRAKV NDLLDFFVSK YGGEETVTFQ RARLNFIHSM AAYSVACYIL QIKDRHNGNI
MIDAEGHIIH IDFGFLFDID KLLGVKFEPS SFKLNAEMVA LMGGRHSQGY DLFQHLTVKG
FLALRPHADQ LVSTVQLMLG TGLPSFKGEI TIRRLKDRFV LGFNDRQAGE WMMGVIRNAH
ENIRSTVYDE FQRVSGS
//
