ID X0C7A4_FUSOX Unreviewed; 1727 AA.
AC X0C7A4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=FOQG_07448 {ECO:0000313|EMBL:EXK90031.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK90031.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK90031.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK90031.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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; JH658376; EXK90031.1; -; Genomic_DNA.
DR HOGENOM; CLU_000893_1_0_1; -.
DR Proteomes; UP000030663; 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; 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:EXK90031.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1157..1344
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1417..1711
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1727 AA; 194005 MW; 83E735A2A8D92278 CRC64;
MIKKIRELLS EPFLIAVETA LSTIRNCHSQ DREVKEWKRY LRHYASSGRP LGAMLLHRSF
AHLIVSSTSL MVKDPRSLRE SHVLDIYIAQ GEDLCNIASS ALEADFKTVE EYAALAIEEI
QYIEGGADFI RMGSPDQQSL AYAVKAAALI SYLNCALLNE DAADTEILMN WLQETLDDSV
QMADPTLASV TLRCLALICQ ISPSFSSNVS RILPRFIVQD APQKDIVTIA SNSLAYALKM
LSKDAVIGTL YTLGNVLSPG SDQAFVNDQI DGTASETGLN AIYTNRRSIG SSISLQMYGE
EETAIVSGNV VQTICGIAAA FKDEKITALA QSMLQQKLEK VNTGVDARII SGAAALALEG
GQLEFRSLLK LFSKLCHTGV VENQLFLLEA VRNARTFISA NLRRDSQLFG IYYEHLLDSI
IGLGDVHSSG HTKESDVQMA AKEIAELLHP LAIFMSTNDF AFEPIADDET YSLLRDAWFN
IVVHGFTTNT DRGKQYMREL RMIAIHSPPL VAEQRGEQVE SDIELNTVLR RGMSNDRESL
QKKLLSDLVP SKSNEIRSLS YRKVIFLQAA YLMEILRADS GDCTKVLSYF LEPSMSKGEL
SSAMEGVAAA VMDKYIQKTQ SGAEPTFSAQ YAAEQLATIF CSCCHRIERV QQAAFVCADR
FLREIPSALC YRSSLFALIE LLSLMWSSCL EAETDVYAPR STFTSELGGV TVQLSDDYDF
RRWTVDILNR KARVWVNSAI NLSPLDVKGI LQTYLSEFSD EGAYGHVSLG RSFALELGSI
IPSTDNRLQS MDKIGNSSVN TASAFVAQYT TRQEYRYGET LPDRGTELMS FMNHNRRLSF
VQSSVKESAN ATTALAHIEA RILSKKSTSI TEVRDILRRA AALLCRTSKD EAAVAHHLVS
IPFALFTKQS INLGVSLWLG VINENPRQES RLLNEIVQQW EFTLTRKVGL FSPTLNHVDP
FFLKEEFAPS ELEALAKKKQ IVHDILSPHT RLLQFFASHY NATRLGSPDI QKVFLRMIDL
TLEAMKQSAT HPMAREIRFQ IVLFGLRVLR SSTTLKPAAQ WRLKERLLTA GLSWFRSAPK
WSFGSNLLQM KTEIRLISDV LAALQQVSFI GAQTVGNVKS LQSKEQLLDL LLRNEQLRLI
VWVNPLNNAS NQALTQTAGK APTEAALLPL IRTAWWQDPA IAIELATRFP FPRLQRDIRF
LLLTMPEKAI FEPEALHLIF GGFLPDDVAS QQLKYLLYWE PVNPVTAVTM FLPAYQSHPF
IIQYAMRALE SHSVDVTFFY VPQIVQSLRY DSLGYVKRYI LETAQFSQLF AHQIIWNMKA
NSYKDDDAQI PDEIKPTLDT VMTQMVDGFA AEDRDFYEKE FSFFDEVTDI SGKLKPFIKK
SKPEKKQKIE EELRKIKVEV GVYLPSNPDG VVIGIDRKSG KPLQSHAKAP YMATFRIQKN
KGGVSEVDEM MEENDGEDHG TPERTVEVWQ SAIFKVGDDC RQDVLALQMI AAFRGIFHDV
GLDVYVFPYR VTATAPGCGV IDVLPNSISR DMLGREAVNG LYDYFISKYG NENSLRFQRA
RSNFVKSMAA YSVISYLLQF KDRHNGNIMI DDAGHILHID FGFCFDIAPG GIKFERAPFK
LTTEMVAVMG GSMEHQSFKA FEELCVKAFL ASRQYCEKLS QIVWLMMDSG LPCFKPESVK
HFRERFVLDK SERDAANFMK HLIKTSYSSH STGIYDQFQL LTNGIPY
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