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Database: UniProt
Entry: U5HEL2_USTV1
LinkDB: U5HEL2_USTV1
Original site: U5HEL2_USTV1 
ID   U5HEL2_USTV1            Unreviewed;      1910 AA.
AC   U5HEL2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=MVLG_05555 {ECO:0000313|EMBL:KDE03986.1};
OS   Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS   smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE03986.1};
RN   [1] {ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA   Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA   Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA   Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KDE03986.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE03986.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA   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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KDE03986.1, ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE03986.1}, and p1A1 Lamole
RC   {ECO:0000313|Proteomes:UP000017200};
RX   PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA   Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA   Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA   Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA   Hood M.E., Schultz D.J., Cuomo C.A.;
RT   "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT   lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT   fungus.";
RL   BMC Genomics 16:461-461(2015).
RN   [4] {ECO:0000313|EnsemblFungi:MVLG_05555T0}
RP   IDENTIFICATION.
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; AEIJ01000585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL541719; KDE03986.1; -; Genomic_DNA.
DR   STRING; 683840.U5HEL2; -.
DR   EnsemblFungi; MVLG_05555T0; MVLG_05555T0; MVLG_05555.
DR   HOGENOM; CLU_000893_0_1_1; -.
DR   InParanoid; U5HEL2; -.
DR   OMA; TIEVWQS; -.
DR   OrthoDB; 147843at2759; -.
DR   Proteomes; UP000017200; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1335..1521
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          1630..1892
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1910 AA;  210911 MW;  175691A6710E12E4 CRC64;
     MDYLDSNLHS AILSSLAANL ASSSTHDDVH LLTESFAGIQ PVTNGVIGGV LNRINGDSHT
     ASGGAHTLIT LSQVDGIIAF CDYAAKAPAK SDNLNRLLVL LQGAPNWQLE AAVGVQVAQD
     YAPGDRLAYS LVSAALIVAG ASPNERTAAL GVLSQFHKAL LAAIETSEGH RIIGYLLPAL
     NGARRAVGNS PFPWTVHDEL PLTPEPSRDL VESVVAAIAY EWDPSTEGGR VALATLKQYD
     SSMRGLSPGL IALVQIEFEL AYWTSAIVPA VKSGGGWRAL LEGDPASITA GGQAAYASAT
     RAHGTFENTY TMLERMDGEY PPDPYAFDVL LSSLKLAVVA TIATGSPTQI LAKLFDDLLT
     HPATVVDEPL QTGAVESLQV FARAFPSTLP TALNTIRNFI SSPSPVLEQS GVLAPSSTMI
     AASACYASLI NLSTNPALRE SAIQSLLNHF VVPEREPLVR QGDVVANDAK SIRSLQEAMS
     DPIKVSVSSN VVHAVARLAL TFKDEQITTL VTSILLQRLV GTSPVVDGAI LFELSELATI
     VNADTFADIL AGISRVSKHA KQDEAMSQTL LNAQTRLAIA ASSRQKFHVK YLSETLALFV
     EEGGAGDRKT TASERAAGLL NLVPILDAFL TGAKFDSRQD VDGSLVSLFR SAWYLIVLSG
     FVSTPSRIAD WQRAALVRIA QRTPGLLRGI KDDFVATELD FNPILRNKEH VLSPDAARQE
     LAAILPSAAS FARSLPAPQV VFLLTVVRLE SLRAEAGQPS IVLSYFHVQG INENPQLYAL
     MTSIAEHVNN TFVSRLSQLV TGHTMDPAVY HEVREILLQC CHTLGKVRTT AIRYLNDLFT
     SFPSLLCSGE VVSTMLELLT VTRRACLAEF VDEYTPLYRF HSSRANFDVV LPDDYSIRNS
     VLTELHRYAR SWLKAGLTRA PSEMRGLLQD YIDGTEVAPP TTSLKAFADD EMGKSVAIDL
     IRMPPSNARE ASLPAWGEWR ADNSSNFART FGAKSFFGGE ASRTADTSRD AILDELEALA
     EQLDQHKMHV KLVDIRALLY RSGGHLVKAQ SPDPDILQQL VHLPARIFTD VVIEIATEVW
     TWVVDARPEL EPRLMVEVAE AWQSTIQRRQ GLFSCEANRK NPLDVSTQFT PTDKDYMTKE
     FIHATRLLQP HMTLLQFLSS RFQAFRYRDT DLVHACMRIL KRSTDAAKSW STHQLAREIR
     MRMLSFGFCV LQGSELESAV EYNFRDSLYE AAMTWFELPP GWTYGSNRIQ LKADLQAMEE
     LHSTIKSDKP AYDYILSASR SRKASGLPYN SSAATAGSLQ TRRQQLLLAL LENEMDRLKL
     WTNPLLDPKR GAIPTPRSTA SDANWVRMAN IAWSHWPGVA VQLPERTKLP AVAAEVTRLV
     RSNPLRAQHI PDALQYFVGD KISPESERHL RVLLFWAPVS VISALRFLFP LFEGDPILLQ
     YALRVLEHHP VEITFFYIPQ VVQALRFDEL GYAERFIFET SKISQLFCHQ IIWNMKANAY
     RGDDGDVEDP MKPTLDRMVD MIVSSLSGDA KDFFQREFAF FNEVTSISAK LKPFIKSSKH
     EKKAKIDEEM AKIKVDVGVY LPSNPDGIVV DVDRKSGRPL QSHAKAPFMA TFKVRRDHKR
     SVTADLDAQD ALIEDGESSG QVQPKSFDTW QSAIFKVGDD CRQDVLALQI IAMHKNIFTA
     LGLDLLVTPY RVTATGPGCG VIDVIPNATS RDEMGRAKVN DLKSFFVLKY GSPDGIEFQR
     ARNNFIQSMA AYSLLCYIVQ IKDRHNGNIM IDGKGCITHI DFGFLFDIGP GGVKFEPSSF
     KLSHEMMVLM GGKDSVGFRH FSELTVKSFL ACRPYAQQIV DTARLMLAAE FPSFKGEPTM
     QRLTERFRLE LREDEAAEYM KGVIANAHEN PRSIVYDIFQ EKTNGIPYVR
//
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